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关节炎疾病造模试剂,疾病检测试剂
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Immunization Grade Chick Type IX Collagen, 5 mg, lyophilized

Immunization Grade Chick Type IX Collagen, 5 mg, lyophilized

Immunization Grade Chick Type IX Collagen, 5 mg, lyophilized

报价:0.00

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中文名称:
Immunization Grade Chick Type IX Collagen, 5 mg, lyophilized
英文名称:
Immunization Grade Chick Type IX Collagen, 5 mg, lyophilized
品牌:
Chondrex
货号:
1071
规格:
5mg
报价:
0.00
保存温度:
4℃,inthedark
说明书:
DESCRIPTION: Type IX collagen purified from pepsin-solubilized articular chick cartilage by repeating salt precipitation. Type IX collagen is one of three types of collagen composing cartilage fibrils. Type IX collagen consists of three genetically distinct polypeptides, which are cross-linked by disulphide bonds, and is digested into two fragments, highmolecular weight (HMW) and lowmolecular weight (LMW) fragments by pepsindigestion for solubilization from tissues. The ratio of HMW and LMW varies between individual batches.
APPLICATION: Use as an immunizing antigen to generate antibodies, as an ELISAantigen to detect anti-type IX collagen antibodies and as a standard for gel analysis. Note: Anti-type IX collagen antibodies which cross-react to autologous type IX collagenmay contribute the induction of polychondritis in certain strains of mice.
QUANTITY: 5 mg
FORM: Lyophilized powder
SOURCE: Chick
MOLECULAR WEIGHT: Intact type IX collagen: approximately 220 Kd, by 8% gel analysis under non-reduced conditions, pepsinsolubilized type IX collagen is a mixture of three HMW (150, 135 and 120 Kd) and one LMW (35 Kd) fragments.
PURITY: >90% by SDS-PAGE
SOLUBILITY: Type IX collagen can be dissolved at 4 mg/ml in acidic solution such as 0.01-0.05M acetic acid, pH 3.0-3.3 or 0.15M citrate buffer, pH 3.6 by stirring at 4°C overnight. To neutralize the solution, add 10X neutral buffer containing 1.5M NaCl or dialyze the solution against a neutral buffer.
STORAGE TEMPERATURE: 4°C in the dark for lyophilized formand –20°C for solution. Collagenmight be gradually degraded under neutral conditions.
STABILITY: 2 years
REFERENCES: 1.Shimokomaki M, Duance VC, Bailey AJ. FEBS Lett. 121:51-54 (1980)
2.Reese CA, Wiedemann H, Kuhn K, Mayne R. Biochemistry: 21:826-830 (1982)
3.vander Rest M, Mayne R, Ninomiya Y et al. J Biol Chem. 260:220-225 (1985)

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