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| Product | Description | |
|---|---|---|
| coagulation factor Xa | A blood coagulation factor formed from the proenzyme factor X by limited proteolysis. Factor X is a glycoprotein composed of a heavy chain and a light chain, which are generated from a precursor protein by the excision of the tripeptide RKR and held together by one or more disulfide bonds. The activated factor Xa converts prothrombin to thrombin in the presence of factor Va, Ca2+ and phospholipids. Scutelarin (EC 3.4.21.60) has similar specificity, but does not require factor Va. Group: Enzymes. Synonyms: thrombokinase; prothrombase; prothrombinase; activated blood-coagulation factor X; autoprothrombin C; thromboplastin; plasma thromboplastin; factor Xa; activated Stuart-Prower factor; activated factor X. Enzyme Commission Number: EC 3.4.21.6. CAS No. 9002-5-5. Factor Xa. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4150; coagulation factor Xa; EC 3.4.21.6; 9002-05-5; thrombokinase; prothrombase; prothrombinase; activated blood-coagulation factor X; autoprothrombin C; thromboplastin; plasma thromboplastin; factor Xa; activated Stuart-Prower factor; activated factor X. Cat No: EXWM-4150. |  |
| coagulation factor XIIa | Also activates plasminogen and plasma prokallikrein. Formed from the proenzyme, factor XII, by plasma kallikrein or factor XIIa. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: Hageman factor (activated); blood-coagulation factor XIIf; activated β blood-coagulation factor XII; prealbumin activator; Hageman factor β-fragment; Hageman factor fragment HFf; blood-coagulation factor XIIaβ; prekallikrein activator; kallikreinogen activator. Enzyme Commission Number: EC 3.4.21.38. CAS No. 75216-42-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4132; coagulation factor XIIa; EC 3.4.21.38; 75216-42-1; Hageman factor (activated); blood-coagulation factor XIIf; activated β blood-coagulation factor XII; prealbumin activator; Hageman factor β-fragment; Hageman factor fragment HFf; blood-coagulation factor XIIaβ; prekallikrein activator; kallikreinogen activator. Cat No: EXWM-4132. | |
| complement subcomponent C1r | Activated from proenzyme C1r in plasma during activation of the complement system by the "classical" route. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: activated complement C1r; C1r esterase; activated complement C1r. Enzyme Commission Number: EC 3.4.21.41. CAS No. 80295-69-8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4135; complement subcomponent C1r; EC 3.4.21.41; 80295-69-8; activated complement C1r; C1r esterase; activated complement C1r. Cat No: EXWM-4135. | |
| complement subcomponent C1s | Activated from proenzyme C1s in plasma by complement subcomponent C1r. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: C1 esterase; activated complement C1s; complement C1r. Enzyme Commission Number: EC 3.4.21.42. CAS No. 80295-70-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4136; complement subcomponent C1s; EC 3.4.21.42; 80295-70-1; C1 esterase; activated complement C1s; complement C1r. Cat No: EXWM-4136. | |
| Matrix Metalloproteinase-3 from Human, Recombinant | Matrix metalloproteinase-3 (MMP-3) also known as stromelysin-1 and transin (EC 3.4.24.17) cleaves a number of substrates including cartilage proteoglycan, collagen types II, III, IV, V and IX, fibronectin, laminin, and can activate MMP 1. MMP-3 is secreted as 57 and 59 kDa proenzymes and can be activated in vitro by organomercurials (e.g., 4 aminophenylmercuric acetate, APMA) and in vivo by proteases via intermediate forms to a 45 kDa active MMP 3 enzyme. Further autolysis to a 28 kDa form can also occur. MMP-3 is thought to play an important role in pathophysiological degradation processes associated with conditions such as rheumatoid arthritis and cancer cell invas...C 3.4.24.17; matrix metalloproteinase 3; proteoglycanase; collagenase activating protein; procollagenase activator; transin; MMP-3; neutral proteoglycanase; stromelysin; collagen-activating protein. Enzyme Commission Number: EC 3.4.24.17. CAS No. 79955-99-0. Purity: >95% by SDS-PAGE. Matrix Metalloproteinase. Mole weight: 57 kDa. Storage: < -70°C; Avoid freeze/thaw. Form: Lyophilized from 100 mM NaCl, 50 mM HEPES, pH 7.3. Species: Human. Stromelysin 1; EC 3.4.24.17; matrix metalloproteinase 3; proteoglycanase; collagenase activating protein; procollagenase activator; transin; MMP-3; neutral proteoglycanase; stromelysin; collagen-activating protein. Cat No: NATE-0861. | |
| meprin B | A brush border membrane-bound metalloendopeptidase known from the intestine of all mouse strains that have been tested, and the kidney of certain inbred strains. A tetramer of meprin β subunits (in contrast to meprin A, which contains both α and β subunits). Occurs in the kidney as a proenzyme that can be activated by trypsin. Meprin B is inhibited by both EDTA and 1,10-phenanthroline, but not by phosphoramidon, captopril or thiorphan. In peptidase family M12 (astacin family). Group: Enzymes. Synonyms: meprin-b. Enzyme Commission Number: EC 3.4.24.63. CAS No. 150679-52-0. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4346; meprin B; EC 3.4.24.63; 150679-52-0; meprin-b. Cat No: EXWM-4346. | |
| protein C (activated) | A peptidase of family S1 (trypsin family), one of the γ-carboxyglutamic acid-containing coagulation factors. Formed from protein C, the proenzyme that circulates in plasma, by the action of a complex of thrombin with thrombomodulin, or by serine endopeptidases present in several snake venoms. Group: Enzymes. Synonyms: blood-coagulation factor XIVa; activated blood coagulation factor XIV; activated protein C; autoprothrombin II-A; protein Ca; APC; GSAPC. Enzyme Commission Number: EC 3.4.21.69. CAS No. 42617-41-4. Protein C. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4160; protein C (activated); EC 3.4.21.69; 42617-41-4; blood-coagulation factor XIVa; activated blood coagulation factor XIV; activated protein C; autoprothrombin II-A; protein Ca; APC; GSAPC. Cat No: EXWM-4160. | |
| alternative-complement-pathway C3/C5 convertase | A bimolecular complex of complement fragment Bb with either C3b or cobra venom factor; Bb contains the active site. Bb is formed by cleavage of proenzyme factor B by factor D. Cleavage of complement component C5 requires additional C3b which binds C5 and renders it susceptible to cleavage by C3b,Bb complex. C3b,Bb is stabilized in plasma by factor P. Complement factor B is in peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: complement component C3/C5 convertase (alternative); proenzyme factor B; properdin factor B; C3 proactivator; glycine-rich β-glycoprotein; heat-labile factor; C3 convertase; C3. Enzyme Commission Number: EC 3.4.21.47. CAS No. 80295-67-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4140; alternative-complement-pathway C3/C5 convertase; EC 3.4.21.47; 80295-67-6; complement component C3/C5 convertase (alternative); proenzyme factor B; properdin factor B; C3 proactivator; glycine-rich β-glycoprotein; heat-labile factor; C3 convertase; C3b,Bb,CVF,Bb,C5 convertase; (C3b)n,Bb; complement C 3(C 5) convertase (amplification); alternative complement pathway C3(C5) convertase; C5 convertase; CVF,Bb; (CVF)-dependent glycine-rich-β-glucoprotein; cobra venom factor-dependent C3 convertase. Cat No: EXWM-4140. | |
| bontoxilysin | This zinc enzyme, produced by Clostridium botulinum, occurs as forms A-G that differ in specificity of action on the proteins of the neuroexocytosis apparatus. The 150-kDa proenzymes of bontoxilysin are processed to disulfide-linked subunits of 100 and 50 kDa, the latter being responsible for the endopeptidase activities. Weakly inhibited by captopril, and phosphoramidon. Toxicity is due to action at the neuromuscular junctions that blocks release of acetylcholine, causing flaccid paralysis, in contrast to the spastic paralysis caused by tentoxilysin. In peptidase family M27 (tentoxilysin family). Group: Enzymes. Synonyms: botulinum neurotoxin; BoNT. Enzyme Commission Number: EC 3.4.24.69. CAS No. 107231-12-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4352; bontoxilysin; EC 3.4.24.69; 107231-12-9; botulinum neurotoxin; BoNT. Cat No: EXWM-4352. | |
| Carboxypeptidase-B rat, Recombinant | Carboxypeptidase B (or peptidyl-L-lysine (-L-arginine) hydrolase) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. It has been shown to be a single polypeptide of 34 kDa Da. Trypsin is capable of converting native enzyme to the active enzyme, carboxypeptidase B II in vitro. The optimum pH is found to be 9.0. The enzyme may be used for sequence analysis by successive cleavage of C-terminal basic amino acids. It can also be used as a serum marker for the diagnosis of acute pancreatitis. Caspase 3 is synthesized as a 32 kda proenzyme. the active enzyme is a heterodimer of two large (17 kda) subunit...sponsible for rapidly metabolizing the c5a protein into c5a des-arg, with one less amino acid. Group: Enzymes. Synonyms: carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Enzyme Commission Number: EC 3.4.17.2. CAS No. 9025-24-5. CPB1. Activity: 50-55 units/mg protein carboxypeptidase B. Storage: -20°C. Form: Lyophilized from 20 mM Tris, pH 8.0 + 50 mM NaCl. Source: E. coli. Species: Rat. carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Cat No: NATE-0153. | |
| Caspase-6 (Active) from Human, Recombinant | Caspase-6 is an enzyme that in humans is encoded by the CASP6 gene. This gene encodes a protein that is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes that undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein is processed by caspases 7, 8 and 10, and is thought to function as a downstream enzyme in the caspase activation cascade. Caspase 6 can also undergo self-processing without other members of the caspase family. Alternative splicing of this gene results in two transcript variants that encode different isoforms. Group: Enzymes. Synonyms: CASP6; MCH2; Caspase-6 (Active); Caspase-6. Caspase 6. Appearance: Liquid. Storage: -80°C. Form: Liquid. 5μg in 25μl of 50mM TRIS (pH 8.0) containing 100mM sodium chloride and 50mM imidazole. Source: E. coli. Species: Human. CASP6; MCH2; Caspase-6 (Active); Caspase-6. Cat No: NATE-0814. | |
| Caspase-7 from Human, Recombinant | Caspase-7 is a member of the caspase (cysteine aspartate protease) family of proteins, and has been shown to be an executioner protein of apoptosis. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes that undergo proteolytic processing by upstream caspases (caspase-8, -9) at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme in the form of a heterotetramer. The precursor of this caspase is cleaved by caspase 3, caspase 10, and caspase 9. It is activated upon cell death stimuli and induces apoptosis. Alternative splicing results in four transcript variants, encoding three distinct isoforms. Applications: Used to screen caspase inhibitors, study enzyme regulation, determine caspase substrate specificity, or as positive control in caspase activity assays. Group: Enzymes. Synonyms: CASP7; CASP-7; CMH-1; ICE-LAP3; LICE2; MCH3; Caspase-7. Enzyme Commission Number: EC 3.4.22.-. Purity: 90% (SDS-PAGE). Caspase 7. Activity: ~25,000U/mg protein. Appearance: Lyophilized. Storage: -80°C. Source: E. coli. Species: Human. CASP7; CASP-7; CMH-1; ICE-LAP3; LICE2; MCH3; Caspase-7. Cat No: NATE-0815. | |
| cathepsin X | Cathepsin X is a lysosomal cysteine peptidase of family C1 (papain family). The pH optimum is dependent on the substrate and is 5.0 for the carboxypeptidase activity. Unstable above pH 7.0. Compound E-64, leupeptin and antipain are inhibitors, but not cystatin C. Cathepsin X is ubiquitously distributed in mammalian tissues. The propeptide is extremely short (38 amino acid residues) and the proenzyme is catalytically active. Human gene locus: 20q13. Group: Enzymes. Synonyms: cathepsin B2; cysteine-type carboxypeptidase; cathepsin IV; cathepsin Z; acid carboxypeptidase; lysosomal carboxypeptidase B. Enzyme Commission Number: EC 3.4.18.1. CAS No. 37217-21-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4081; cathepsin X; EC 3.4.18.1; 37217-21-3; cathepsin B2; cysteine-type carboxypeptidase; cathepsin IV; cathepsin Z; acid carboxypeptidase; lysosomal carboxypeptidase B. Cat No: EXWM-4081. | |
| classical-complement-pathway C3/C5 convertase | A complex of complement fragments C4b, C2a and C2b. C2a contains the active site, C2b the site for C4b binding. C2a and C2b are formed by cleavage of proenzyme C2 by complement subcomponent C1s. Cleavage of C5 requires complement fragment C3b which binds C5 and renders it susceptible to cleavage by the C4b,2a complex. Includes former EC 3.4.21.44. Complement component C2a is in peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: C3 convertase; C42; C4b,2a; C5 convertase; C423; C4b,2a,3b; C42; C5 convertase; C423; C4b,2a,3b; complement C.hivin.4.hivin2; complement C3 convertase. Enzyme Commission Number: EC 3.4.21.43. CAS No. 56626-15-4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4137; classical-complement-pathway C3/C5 convertase; EC 3.4.21.43; 56626-15-4; C3 convertase; C42; C4b,2a; C5 convertase; C423; C4b,2a,3b; C42; C5 convertase; C423; C4b,2a,3b; complement C.hivin.4.hivin2; complement C3 convertase. Cat No: EXWM-4137. | |
| coagulation factor IXa | A chymotrypsin homologue, and one of the γ-carboxyglutamic acid-containing blood coagulation factors. The proenzyme factor IX is activated by factor XIa. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: activated Christmas factor; blood-coagulation factor IXa; activated blood-coagulation factor IX; autoprothrombin II; blood platelet cofactor II; activated blood coagulation factor XI. Enzyme Commission Number: EC 3.4.21.22. CAS No. 37316-87-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4122; coagulation factor IXa; EC 3.4.21.22; 37316-87-3; activated Christmas factor; blood-coagulation factor IXa; activated blood-coagulation factor IX; autoprothrombin II; blood platelet cofactor II; activated blood coagulation factor XI. Cat No: EXWM-4122. | |
| coagulation factor XIa | In peptidase family S1 (trypsin family), and one of the γ-carboxyglutamic acid-containing blood coagulation factors. The proenzyme factor XI is activated by factor XIIa. Group: Enzymes. Synonyms: blood-coagulation factor XIa; activated blood-coagulation factor XI; activated plasma thromboplastin antecedent. Enzyme Commission Number: EC 3.4.21.27. CAS No. 37203-61-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4125; coagulation factor XIa; EC 3.4.21.27; 37203-61-5; blood-coagulation factor XIa; activated blood-coagulation factor XI; activated plasma thromboplastin antecedent. Cat No: EXWM-4125. | |
| leishmanolysin | A membrane-bound glycoprotein found on the promastigote of various species of Leishmania protozoans. Contains consensus sequence for a zinc-binding site; Z-Tyr-Leu-NHOH is a strong inhibitor. The enzyme can activate its proenzyme by cleavage of the Val100?Val bond. An acid pH optimum is found with certain protein substrates. Type example of peptidase family M8. Group: Enzymes. Synonyms: promastigote surface endopeptidase; glycoprotein gp63; Leishmania metalloproteinase; surface acid proteinase; promastigote surface protease. Enzyme Commission Number: EC 3.4.24.36. CAS No. 161052-06-8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4318; leishmanolysin; EC 3.4.24.36; 161052-06-8; promastigote surface endopeptidase; glycoprotein gp63; Leishmania metalloproteinase; surface acid proteinase; promastigote surface protease. Cat No: EXWM-4318. | |
| macrophage elastase | This enzyme is synthesized as a proenzyme of 53 kDa that is converted to an active form of 22 kDa. cDNA sequences have been obtained for the mouse and human enzymes. In peptidase family M10 (interstitial collagenase family). Group: Enzymes. Synonyms: metalloelastase; human macrophage metalloelastase (HME). Enzyme Commission Number: EC 3.4.24.65. CAS No. 9004-6-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4348; macrophage elastase; EC 3.4.24.65; 9004-06-2; metalloelastase; human macrophage metalloelastase (HME). Cat No: EXWM-4348. | |
| Pro-Urokinase from Human, recombinant | Urokinase or Urokinase-type plasminogen activator (uPA) is a serine protease (EC 3.4.21.73). It is secreted as a single-chain zymogen, pro-Urokinase, possessing little or no intrinsic enzymatic activity. The single chain zymogen is converted into the active two chain enzyme (tcuPA) by cleavage of the bond between Lys157 and Ile158. After activation, Urokinase specifically cleaves the proenzyme plasminogen to form the active enzyme plasmin. The active plasmin then catalyzes the breakdown of fibrin polymers of blood clots. Urokinase is involved in a number of biological functions including fibrinolysis, embryogenesis, cell migration, tissue remodeling, ovulation, and wound healing. Additionally, it is a potent marker of invasion and metastasis in a variety of human cancers associated with breast, stomach, colon, bladder, ovary, brain and endometrium. Group: Enzymes. Synonyms: Single chain Urokinase-type plasminogen activator; s. Purity: > 90% by SDS-PAGE. Pro-Urokinase. Mole weight: 49.3 kDa. Activity: >1200 mU/mg. Storage: Stable at -80°C for at least 1 year as supplied. Store reconstituted aliquots at -80°C. Avoid repeated freeze and thaw cycles. Form: Lyophilized powder. Source: E. coli. Species: Human. Single chain Urokinase-type plasminogen activator; scuPA; Urokinase-type Plasminogen Activator uPA; PLAU; Pro-Urokinase. Cat No: NATE-1689. | |
| tentoxilysin | Zinc enzyme produced by Clostridium tetani. Proenzyme of 150 kDa is processed to disulfide-linked subunits of 100 and 50 kDa, the latter being responsible for the endopeptidase activity. Weakly inhibited by captopril, and phosphoramidon. The clostridial neurotoxins disable the neuroexocytosis apparatus, and have been described as the most toxic substances known. Tentoxilysin acts at the spinal inhibitory interneurons, blocking the release of various neurotransmitters to produce spastic paralysis. Type example of peptidase family M27 (tentoxilysin family). Group: Enzymes. Synonyms: tetanus neurotoxin. Enzyme Commission Number: EC 3.4.24.68. CAS No. 107231-12-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4351; tentoxilysin; EC 3.4.24.68; 107231-12-9; tetanus neurotoxin. Cat No: EXWM-4351. | |
| Tissue plasminogen activator from Human, Recombinant | Tissue plasminogen activator (abbreviated PLAT or tPA) is a secreted serine proteasewhich converts the proenzymeplasminogento plasmin, a fibrinolyticenzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin. This enzyme plays a role in cell migrationand tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysiswhich can result in thrombosisor embolism. Tissue plasminogen activator human recombinant produced in cho cells is a single, glycosylated polypeptide chain containing 527 amino acids and having a mol...0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. tPA. Mole weight: 59008.71 Da. Activity: 580,000 IU/mg. Stability: Lyophilized t-PA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution tPA should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles. Appearance: Sterile Filtered White lyophilized (freeze-dried) powder. Source: CHO. Species: Human. Tissue-type plasminogen activator; EC 3.4.21.68; tPA; t-PA; t-plasminogen activator; TPA; T-PA. Cat No: NATE-0920. | |
| Urokinase from Human, recombinant | Urokinase or Urokinase-type plasminogen activator (uPA) is a serine protease (EC 3.4.21.73). It is secreted as a single-chain zymogen, pro-Urokinase, possessing little or no intrinsic enzymatic activity. The single chain zymogen is converted into the active two chain enzyme (tcuPA) by cleavage of the bond between Lys157 and Ile158. After activation, Urokinase specifically cleaves the proenzyme plasminogen to form the active enzyme plasmin. The active plasmin then catalyzes the breakdown of fibrin polymers of blood clots. Urokinase is involved in a number of biological functions including fibrinolysis, embryogenesis, cell migration, tissue remodeling, ovulation, and wound healing. Additionally, it is a potent marker of invasion and metastasis in a variety of human cancers associated with breast, stomach, colon, bladder, ovary, brain and endometrium. Group: Enzymes. Synonyms: Two chain urokinase-type plasminogen acti. Enzyme Commission Number: EC 3.4.21.73. Purity: > 90% by SDS-PAGE. uPA. Mole weight: 49.3 kDa. Activity: >1500 mU/mg. Storage: Stable at -80°C for at least 1 year as supplied. Store reconstituted aliquots at -80°C. Avoid repeated freeze and thaw cycles. Form: Lyophilized powder. Source: E. coli. Species: Human. Two chain urokinase-type plasminogen activator; tcuPA; PLAU; ATF; UPA; URK; u-PA; BDPLT5; QPD; Urokinase. Cat No: NATE-1690. | |
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