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HSPD1 (基因名), 60 kDa heat shock protein, mitochondrial (蛋白名), ch60_human.

产品名称:

HSPD1 Antibody

货号:

P0822Rb-h

商标:

EIAab^®

监管等级:

RUO

别名:

60 kDa chaperonin, Chaperonin 60, Heat shock protein 60, HuCHA60, Mitochondrial matrix protein P1, P60 lymphocyte protein, CPN60, HSP-60, HSP60

序列号:

P10809

反应性:

human

免疫原:

Recombinant human HSPD1 protein ( R0822h )

形态:

Liquid

存储说明:

4℃ for frequent use, -20℃ to -70℃ for 6 months

缓冲液:

0.1M×PBS,50% glycerol,pH7.5

浓度:

200ug/ml

纯化方式:

Immunogen affinity purified

克隆性:

Polyclonal

亚型:

Rabbit IgG

应用:

推荐产品:

Goat Anti-Rabbit IgG(H+L) HRP-conjugated Antibody

研究领域:

Epigenetics

规格 & 价格:

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Human HSPD1 Polyclonal Antibody

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产品说明书

数据表:

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R&D 技术数据

Immunohistochem1 of paraffin-embedded human testis using HSPD1 antibody.

通用注释

亚单元:

(Microbial infection) Interacts with HBV protein X and HTLV-1 protein p40tax (PubMed:15120623, PubMed:1731090).

功能:

Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (PubMed:1346131, PubMed:11422376). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein.

亚细胞位置:

Mitochondrion matrix

数据库链接

UniGene:

Hs.595053

SMR:

P10809

STRING:

9606.ENSP00000340019

KEGG:

hsa:3329

MIM: