Skip to Content
MilliporeSigma

Skip To

SAE0049

L-Lactate Dehydrogenase (LDHA)

from human, recombinant, expressed in E. coli, aqueous solution

Synonym(s):

Lactic Dehydrogenase, recombinant from E. coli, α-HBDH, α-hydroxy butyratede hydrogenase, anaerobic lactate dehydrogenase, (S)-Lactate: NAD+ oxidoreductase, L-Lactate Dehydrogenase, Lactate

Sign In to View Organizational & Contract Pricing.

Select a Size

Change View
Size/SKUAvailabilityPrice
10 kU

Available to ship TODAYfromMILWAUKEE

$456.00

About This Item

CAS Number:
UNSPSC Code:
12352200
NACRES:
NA.54
EC Number:
MDL number:
Biological source:
human
Recombinant:
expressed in E. coli

$456.00


Available to ship TODAYDetails


Request a Custom Order
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist


biological source

human

Quality Segment

recombinant

expressed in E. coli

form

aqueous solution

storage condition

(Keep container tightly closed in a dry and well-ventilated place)

color

colorless

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... LDHA(3939)

General description

Research area: Cell Signaling
The gene LDHA (L-lactate dehydrogenase A chain) is mapped to human chromosome 11p15. It is a subunit of lactate dehydrogenase.In particular, lactic dehydrogenase A (LDHA) is mainly found in skeletal muscle, and for that reason is known as the M subunit. This recombinant form of LDHA has a C-terminal histidine-tag.

Application

L-Lactate Dehydrogenase (LDHA) has been used in in vitro phosphoglycerate mutase 1 (PGAM1) inhibitors screening assay. It has also been used in a colorimetric assay for determining lactate concentration in conditioned media.

Biochem/physiol Actions

L-lactic dehydrogenase catalyzes the conversion of L-lactate into L-pyruvate while reducing NAD+ to NADH and H+.
L-lactic dehydrogenase catalyzes the conversion of L-lactate into L-pyruvate while reducing NAD+ to NADH and H+.  L-lactate dehydrogenase A chain (LDHA), an enzyme involved in pyruvate metabolism, LDH is responsible for the conversion of pyruvate to lactate, the final step of glycolysis. It is overexpressed in various cancers. LDHA regulates the microenvironment of developing tumors by the hypoxia-inducible factor (HIF)-signaling pathway. LDHA aids in the NAD+ regeneration during the β-oxidation of fatty acid. LDHA (L-lactate dehydrogenase A chain) is responsible for the conversion of pyruvate to lactate, the final step of glycolysis. It is overexpressed in various cancers. In cancer cells, HIF-1a (hypoxia-inducible factor) induces the expression of LDHA, which helps in maintaining glycolysis in cells.

Physical form

Buffered aqueous solution with Hepes (pH 7.5), NaCl and glycerol.

Other Notes

One unit will reduce 1.0 μmole of pyruvate to L-lactate per min at pH 7.5 at 37 °C.

Compare Similar Items

View Full Comparison

Show Differences

1 of 1

This Item
L7016L125459747
description

from human, recombinant, expressed in E. coli, aqueous solution

description

clone HH-17, ascites fluid

description

Type XI, lyophilized powder, 600-1,200 units/mg protein

description

≥90 U/mg

Gene Information

human ... LDHA(3939)

Gene Information

human ... LDHB(3945)

Gene Information

-

Gene Information

-

biological source

human

biological source

mouse

biological source

rabbit muscle

biological source

-

recombinant

expressed in E. coli

recombinant

-

recombinant

-

recombinant

expressed in E. coli

form

aqueous solution

form

-

form

lyophilized powder

form

powder

UniProt accession no.

P00338

UniProt accession no.

P07195

UniProt accession no.

-

UniProt accession no.

-

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C


Storage Class

10 - Combustible liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable



Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number

It looks like we've run into a problem, but you can still download Certificates of Analysis from our Documents section.

If you need assistance, please contact Customer Support

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library



Questions

Reviews

No rating value

Active Filters