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WH0025813M4

Sigma-Aldrich

Monoclonal Anti-SAMM50 antibody produced in mouse

clone 2A9, purified immunoglobulin, buffered aqueous solution

Synonyme(s) :

Anti-CGI51, Anti-OMP85, Anti-SAM50, Anti-TOB55, Anti-TRG3, Anti-YNL026W, Anti-sorting and assembly machinery component 50 homolog (S. cerevisiae)

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Conjugué

unconjugated

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

2A9, monoclonal

Forme

buffered aqueous solution

Espèces réactives

mouse

Technique(s)

indirect ELISA: suitable
western blot: 1-5 μg/mL

Isotype

IgG2bκ

Numéro d'accès GenBank

BC007830

Numéro d'accès UniProt

Q8BGH2

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... SAMM50(25813)

Description générale

SAMM50 is a component of the sorting and assembly machinery (SAM) complex of the outer mitochondrial membrane. The SAM complex has a role in integrating beta-barrel proteins into the outer mitochondrial membrane (Humphries et al., 2005 [PubMed 15644312]).[supplied by OMIM

Immunogène

SAMM50 (AAH07830, 1 a.a. ~ 468 a.a) full-length recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.

Sequence
MGTVHARSLEPLPSSGPDFGGLGEEAEFVEVEPEAKQEILENKDVVVQHVHFDGLGRTKDDIIICEIGDVFKAKNLIEVMRKSHEAREKLLRLGIFRQVDVLIDTCQGDDALPNGLDVTFEVTELRRLTGSYNTMVGNNEGSMVLGLKLPNLLGRAEKVTFQFSYGTKETSYGLSFFKPRPGNFERNFSVNLYKVTGQFPWSSLRETDRGMSAEYSFPIWKTSHTVKWEGVWRELGCLSRTASFAVRKESGHSLKSSLSHAMVIDSRNSSILPRRGALLKVNQELAGYTGGDVSFIKEDFELQLNKQLIFDSVFSASFWGGMLVPIGDKPSSIADRFYLGGPTSVRGFSMHSIGPQSEGDYLGGEAYWAGLHLYTPLPFRPGQGGFGELFRTHFFLNAGNLCNLNYGEGPKAHIRKLAECIRWSYGAGIVLRLGNIARLELNYCVPMGVQTGDRICDGVQFGAGIRFL

Actions biochimiques/physiologiques

Sorting and assembly machinery (SAM) 50 helps in aggregation of β-barrel proteins into the outer mitochondrial membrane (OMM). SAM 50, along with mitofilin and coiled-coil-helix-coiled-coil-helix domain containing 3 (CHCHD3), plays a vital role in maintaining mitochondrial shape, the morphology of cristae, and the assembly of respiratory complexes. Elevated expression of SAMM50 leads to mitochondrial fragmentation in HeLa cells under the influence of dynamin-related protein (Drp) 1. Depleted expression of SAM 50 affects assembly and steady-state level of voltage-dependent anion-selective channel (VDAC), which is essential for transport of metabolite across OMM.

Forme physique

Solution in phosphate buffered saline, pH 7.4

Informations légales

GenBank is a registered trademark of United States Department of Health and Human Services

Clause de non-responsabilité

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Code de la classe de stockage

10 - Combustible liquids

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Vera Kozjak-Pavlovic et al.
EMBO reports, 8(6), 576-582 (2007-05-19)
Voltage-dependent anion-selective channel (VDAC) is a beta-barrel protein in the outer mitochondrial membrane that is necessary for metabolite exchange with the cytosol and is proposed to be involved in certain forms of apoptosis. We studied the biogenesis of VDAC in
Christine Ott et al.
Molecular and cellular biology, 32(6), 1173-1188 (2012-01-19)
Mitochondria possess an outer membrane (OMM) and an inner membrane (IMM), which folds into invaginations called cristae. Lipid composition, membrane potential, and proteins in the IMM influence organization of cristae. Here we show an essential role of the OMM protein

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