LIF Human, His

Leukemia Inhibitory Factor Human Recombinant, His tag
Cat. No.
BT19199
Source

Escherichia Coli.

Synonyms

CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.

Appearance
Filtered White lyophilized (freeze-dried) powder.
Purity

Greater than 95.0% as determined by SDS-PAGE.

Usage

THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Shipped with Ice Packs
In Stock

Description

LIF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 23-202) containing 189 amino acids including a 9 a.a N-terminal His tag. The total molecular mass is 20.9kDa (calculated).

Product Specs

Introduction
Leukemia Inhibitory Factor (LIF) is a lymphoid factor that supports the prolonged survival of embryonic stem cells by preventing their spontaneous differentiation. LIF plays multiple roles, including promoting the differentiation of cholinergic neurons, regulating stem cell pluripotency, influencing bone and fat metabolism, stimulating the proliferation of factor-dependent cell lines, and enhancing megakaryocyte production in living organisms. Human and mouse LIF share a 78% similarity in their amino acid sequences.
Description
Recombinant Human LIF, produced in E. coli, is a single, non-glycosylated polypeptide chain encompassing amino acids 23 to 202 (a.a 23-202). It consists of 189 amino acids, including a 9-amino acid N-terminal His tag. The calculated molecular mass is 20.9 kDa.
Physical Appearance
White powder, filtered and lyophilized (freeze-dried).
Formulation
LIF is sterile-filtered at 0.4 µm and lyophilized from a 0.5 mg/ml solution in 20 mM Tris buffer, 20 mM NaCl, and 5% w/v trehalose, at a pH of 7.5.
Solubility
To prepare a working stock solution of approximately 0.5 mg/ml, it is recommended to add deionized water and allow the lyophilized pellet to dissolve completely.
Stability
Store the lyophilized protein at -20°C. After reconstitution, aliquot the product to prevent repeated freezing and thawing cycles. The reconstituted protein can be stored at 4°C for a limited period; it remains stable for at least two weeks at 4°C.
Purity
Purity exceeds 95.0%, as determined by SDS-PAGE analysis.
Synonyms

CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.

Source

Escherichia Coli.

Amino Acid Sequence

MKHHHHHHAS PLPITPVNAT CAIRHPCHNN LMNQIRSQLA QLNGSANALF ILYYTAQGEP FPNNLDKLCG PNVTDFPPFH ANGTEKAKLV ELYRIVVYLG TSLGNITRDQ KILNPSALSL HSKLNATADI LRGLLSNVLC RLCSKYHVGH VDVTYGPDTS GKDVFQKKKL GCQLLGKYKQ IIAVLAQAF.

Product Science Overview

Structure and Production

The human recombinant LIF with a His tag is produced in Escherichia coli (E. coli) expression systems. This recombinant protein is a single, non-glycosylated polypeptide chain consisting of 189 amino acids, including a 9-amino acid N-terminal His tag . The molecular weight of this recombinant protein is approximately 20.9 kDa .

Biological Functions

LIF has several important functions:

  • Stem Cell Maintenance: LIF is essential for the long-term maintenance of embryonic stem cells by preventing their spontaneous differentiation .
  • Neuronal Differentiation: It promotes the differentiation of cholinergic neurons .
  • Bone and Fat Metabolism: LIF plays a role in regulating bone and fat metabolism .
  • Immune Response: It can be up-regulated by pro-inflammatory cytokines such as tumor necrosis factor-alpha (TNFα) and interleukin-17 (IL-17), and elevated levels of LIF have been observed in conditions like rheumatoid arthritis, neural injury, systemic inflammation, and tuberculosis .
Applications

Recombinant human LIF is widely used in research and biotechnology for various applications:

  • Stem Cell Research: It is used to maintain the pluripotency of embryonic stem cells in culture .
  • Functional Assays: LIF is employed in functional assays to study its effects on cell proliferation and differentiation .
  • Immunohistochemistry and ELISA: It is used in immunohistochemistry and enzyme-linked immunosorbent assays (ELISA) to detect and quantify LIF levels in biological samples .
Preparation and Storage

The lyophilized recombinant human LIF should be reconstituted in sterile, distilled water or an appropriate buffered solution containing 0.1% bovine serum albumin (BSA) to regain full activity . The reconstituted protein should be apportioned into working aliquots and stored at -20°C to avoid repeated freeze-thaw cycles . The lyophilized protein can be stored at 2-8°C, preferably desiccated .

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