CAPN8 Protein, calpain 8

CAPN8

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CAPN8

Official Full Name calpain 8
Background Calpain proteinases are defined currently as papain like neutral proteases that are calcium activated. Calpains 1 and 2 are composed of a large subunit, which is proteolytically active, and a small subunit (also called calpain 4), or enhancer protein, that is not proteolytically active. The other calpain proteins identified to date are not known to require a small subunit, although there is evidence that the calpain small subunit #2 may act as a chaperonin in the folding of calpains, and then disassociate. Domains in the large subunit include the amino terminal domain I, the proteinase domain II, domain III, and the EF hand domain IV (Domain T in calpains 5 & 6). Calpain 8, also known as NCL 2 (novel calpain 2), was originally characterized in rodents as a stomach specific protein, but the human sequence was isolated from leukocytes. Most similar to calpain 2 (60 % identical to rat or human sequences), murine calpain 8 is also known as a truncated form (Calpain NCL-2), lacking the calcium binding domain, and most of domain III. Homology between human calpain 8 and human calpain 9 (the human stomach specific calpain) is much lower; calpain 9 is more similar to calpain 3. Homology between rat, mouse and human calpain 8 is high. The large subunit of calpain 8 zymogen runs at approximately 80 Kd, and the amino terminal truncation at activation yields an approximately 60 kD form. Cleavage of the carboxyterminal region generates smaller forms of Calpain 8, but it is not clear if these forms are proteolytically active.
Synonyms CAPN8; calpain 8; nCL-2; nCL-2; calpain-8; new calpain 2; stomach-specific M-type calpain; stomach-specific calpain (nCL-2);
    • Species :
    • Mouse
    • Rat
    • Zebrafish
    • Source :
    • Mammalian Cell
    • Tag :
    • His
    Species Cat.# Product name Source (Host) Tag Protein Length Price
    Mouse CAPN8-2699M Recombinant Mouse CAPN8 Protein Mammalian Cell His
    Rat CAPN8-1125R Recombinant Rat CAPN8 Protein Mammalian Cell His
    Zebrafish CAPN8-8055Z Recombinant Zebrafish CAPN8 Mammalian Cell His

    CAPN8 involved in several pathways and played different roles in them. We selected most pathways CAPN8 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with CAPN8 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein

    CAPN8 has several biochemical functions, for example, calcium ion binding, cysteine-type peptidase activity, hydrolase activity. Some of the functions are cooperated with other proteins, some of the functions could acted by CAPN8 itself. We selected most functions CAPN8 had, and list some proteins which have the same functions with CAPN8. You can find most of the proteins on our site.

    Function Related Protein
    calcium ion binding PRKCSH; STIM2; SYT10; BNIP2; LRP1; C2CD4B; PCDHB7; RASGRP3; CAPSL; PCDHGA5
    cysteine-type peptidase activity CASPBL; OTUD5A; CASPB; CASP3A; CLCA5; GM12824; CTSC; SENP7B; USPL1; CAPN1B
    hydrolase activity FHIT; Chil3; PRSS59.1; ALPI.1; CTS7; OVCH2; LTV1; ATP8A1; DESI2; PTPRJA
    metal ion binding KDM5BB; ZNF763; GLIS2B; ZNF558; NUDT10; LMX1BB; ZNF707; TREX1; ASNA1; ZFP36L2
    peptidase activity METAP2A; PRSS44; FAP; CPD; ESPL1; F2RL1.2; IWS1; IMMP2L; PLAUA; KLK1B1

    CAPN8 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with CAPN8 here. Most of them are supplied by our site. Hope this information will be useful for your research of CAPN8.

    Zhang, WD; Ahmad, G; et al. Longevity of Sm-p80-specific antibody responses following vaccination with Sm-p80 vaccine in mice and baboons and transplacental transfer of Sm-p80-specific antibodies in a baboon. PARASITOLOGY RESEARCH 113:2239-2250(2014).
    Renjini, R; Gayathri, N; et al. Analysis of calpain-3 protein in muscle biopsies of different muscular dystrophies from India. INDIAN JOURNAL OF MEDICAL RESEARCH 135:878-886(2012).

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