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Key Documents

WH0025813M4

Sigma-Aldrich

Monoclonal Anti-SAMM50 antibody produced in mouse

clone 2A9, purified immunoglobulin, buffered aqueous solution

Synonym(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

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

2A9, monoclonal

form

buffered aqueous solution

species reactivity

mouse

technique(s)

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

isotype

IgG2bκ

GenBank accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SAMM50(25813)

General description

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

Immunogen

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

Biochem/physiol Actions

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.

Physical form

Solution in phosphate buffered saline, pH 7.4

Legal Information

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

Disclaimer

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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Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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

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