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ATP5G1 Recombinant Rabbit Monoclonal Antibody [JE64-60] (HA722921)

Price: Regular price $385.00

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Catalog# HA722921

Rabbit Monoclonal to ATP5G1

Tested for

  • WB

  • IHC-P

Reacts with

  • Human

  • Mouse

  • Rat

Recombinant production enables lot-to-lot consistency and is animal-cruelty-free

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Specifications

Product Type

Recombinant Rabbit monoclonal primary

Product Name

ATP5G1 Recombinant Rabbit Monoclonal Antibody [JE64-60] (HA722921)

Immunogen

Synthetic peptide within human atp5g1 aa 51-100 / 136.

Host

Rabbit

Positive Control

HeLa cell lysate, Human liver tissue lysate, Mouse liver tissue lysate, Mouse kidney tissue lysate, Rat liver tissue lysate, rat small intestine tissue.

Conjugation

Unconjugated

Clonality

Monoclonal

Clone Number

JE64-60

APPLICATION DILUTION

  • WB

  • 1:5,000

  • IHC-P

  • 1:200

PROPERTIES

Form

Liquid

Storage Condition

Shipped at 4℃. Store at +4℃ short term (1-2 weeks). It is recommended to aliquot into single-use upon delivery. Store at -20℃ long term.

Storage Buffer

1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.

Concentration

1ug/ul

Purification

Protein A affinity purified.

Molecular Weight

Predicted band size: 14 kDa

Isotype

IgG

TARGET

UNIPROT #

P05496

PROTEIN NAME

ATP5G1

SYNONYMS

ATP synthase lipid-binding protein;ATP synthase membrane subunit c locus 1 Imported;ATP synthase proteolipid P1;ATP synthase proton-transporting mitochondrial F(0) complex subunit C1;ATPase protein 9;ATPase subunit c

SUBCELLULAR LOCATION

Mitochondrion membrane.

FUNCTION

Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.

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