Search: 1000 results found for "manf"

Description:

ATPase Inhibitory Factor 1 Human Recombinant

ATPase inhibitor mitochondrial, Inhibitor of F(1)F(o)-ATPase, IF(1), IF1, ATPIF1, ATPI, IP, ATPIP.

Product # :

PRO-1154

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Description

ATPIF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 106 amino acids (26-106 a.a) and having a molecular mass of 12.2kDa.ATPIF1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ATPIF1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
ATPase inhibitory factor 1 (ATPIF1) attaches to the C-terminal region of a beta subunit of the F1-ATPase at low pH values and, through interference of the beta and gamma subunit interaction, ATPIF1 controls the activity of the F1 (the hydrophilic catalytic core), F0 (the membrane embedded protein channel) ATPase. ATPIF1 overexpression in a number of human carcinomas additionally reinforces its participation in oncogenesis and offers insight into the transformed metabolism of cancer cells, including the reprogramming of energy metabolism in relation to glycolysis. Endogenous F1F(o)-ATPase inhibitor curbing ATP depletion when the mitochondrial membrane potential drops below a threshold and the F1F(o)-ATP synthase begins hydrolyzing ATP to pump protons out of the mitochondrial matrix.
Synonyms
ATPase inhibitor mitochondrial, Inhibitor of F(1)F(o)-ATPase, IF(1), IF1, ATPIF1, ATPI, IP, ATPIP.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMGSDQS ENVDRGAGSI REAGGAFGKR EQAEEERYFR AQSREQLAAL KKHHEEEIVH HKKEIERLQK EIERHKQKIK MLKHDD.

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

Description:

Heat Shock Transcription Factor-1 Human Recombinant

HSF-1, HSF1, HSTF-1, HSTF1, Heat shock factor protein 1, Heat shock transcription factor 1.

Product # :

HSP-017

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Description

Recombinant Human HSF1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing a total of 549 amino acids (1-529) and having a molecular mass of 59.4kDa.The HSF1 protein is fused to a 20 aa His-Tag at N-terminus.

Source

Escherichia Coli.

Formulation

The HSF1 protein (1mg/ml) contains 20mM Tris pH-8, 50mM NaCl and 1mM DTT.

Purity

Greater than 75.0% as determined by SDS-PAGE.

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Introduction
The transcription of heat-shock genes is rapidly induced after temperature stress in response to environmental changes, and it is also involved in oogenesis, spermatogenesis, and placental development. Hsp90, is a major repressor of HSF1 gene. HSF1 is known for its participation in heat shock response. HSF1 protein regulates the transcription of hundreds of targets, such as genes involved in protein folding, detoxification, energy generation, carbohydrate metabolism, and cell wall organization.
HSF1 binds to MTA1 in vitro & in breast carcinoma. Suppression of estrogen-dependent transcription may contribute to role of HSF1 in cancer.
Human cancer lines of diverse origins express higher dependence on HSF1 function to maintain proliferation and survival than their non-transformed counterparts.
HSF1 induces anticoagulation and relaxation factors in vascular endothelial cells and could therefore be used to treat cardiovascular disease. HSF1 is directly involved in the regulation of HO1 having an anti-oxidative role.
NF-kappaB and HSF1 are systemically activated in human acute pancreatitis.
HSF1 activation protects against severity of pancreatitis.
HSF is a vital transcription factor which plays a role in up-regulation of VDUP1 expression through stresses such as elevated density and serum deprivation cultures.
Synonyms
HSF-1, HSF1, HSTF-1, HSTF1, Heat shock factor protein 1, Heat shock transcription factor 1.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDLPVGPGAA GPSNVPAFLT KLWTLVSDPD TDALICWSPS GNSFHVFDQG QFAKEVLPKY FKHNNMASFV RQLNMYGFRK VVHIEQGGLV KPERDDTEFQ HPCFLRGQEQ LLENIKRKVT SVSTLKSEDI KIRQDSVTKL LTDVQLMKGK QECMDSKLLA MKHENEALWR EVASLRQKHA QQQKVVNKLI QFLISLVQSN RILGVKRKIP LMLNDSGSAH SMPKYSRQFS LEHVHGSGPY SAPSPAYSSS SLYAPDAVAS SGPIISDITE LAPASPMASP GGSIDERPLS SSPLVRVKEE PPSPPQSPRV EEASPGRPSS VDTLLSPTAL IDSILRESEP APASVTALTD ARGHTDTEGR PPSPPPTSTP EKCLSVACLD KNELSDHLDA MDSNLDNLQT MLSSHGFSVD TSALLDLFSP SVTVPDMSLP DLDSSLASIQ ELLSPQEPPR PPEAENSSPD SGKQLVHYTA QPLFLLDPGS VDTGSNDLPV LFELGEGSYF SEGDGFAEDP TISLLTGSEP PKAKDPTVS.

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

Description:

Interferon Induced With Helicase C Domain 1 Human Recombinant

Interferon-induced helicase C domain-containing protein 1, Clinically amyopathic dermatomyositis autoantigen 140 kDa, CADM-140 autoantigen, Helicase with 2 CARD domains, Helicard, Interferon-induced with helicase C domain protein 1, Melanoma differentiation-associated protein 5, MDA-5, Murabutide down-regulated protein, RIG-I-like receptor 2, RLR-2, RNA helicase-DEAD box protein 116, IFIH1, MDA5, RH116, Hlcd, IDDM19.

Product # :

PRO-1505

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Description

IFIH1 Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 152,000 Dalton. IFIH1 is expressed with a -10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Sf9 Insect Cells.

Formulation

IFIH1 is supplied in 20mM HEPES buffer pH-7.9, 550mM NaCl and 6M Urea.

Purity

Greater than 93.0% as determined by SDS-PAGE.

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Introduction
IFIH1 is a DEAD box protein which is upregulated in response to treatment with beta-interferon and a protein kinase C-activating compound, mezerein. Irreversible reprogramming of melanomas can be attained by therapy with both these agents; treatment with either agent alone only achieves reversible differentiation. DEAD box proteins are implicated in several cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly.
Synonyms
Interferon-induced helicase C domain-containing protein 1, Clinically amyopathic dermatomyositis autoantigen 140 kDa, CADM-140 autoantigen, Helicase with 2 CARD domains, Helicard, Interferon-induced with helicase C domain protein 1, Melanoma differentiation-associated protein 5, MDA-5, Murabutide down-regulated protein, RIG-I-like receptor 2, RLR-2, RNA helicase-DEAD box protein 116, IFIH1, MDA5, RH116, Hlcd, IDDM19.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

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

Description:

Fibroblast Growth Factor-22 Human Recombinant

Fibroblast growth factor 22, FGF-22.

Product # :

CYT-428

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Description

Fibroblast Growth Factor-22 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 149 amino acids and having a molecular mass of 17.3 kDa. The FGF-22 is purified by chromatographic techniques.

Source

Escherichia Coli.

Formulation

The sterile protein powder is lyophilized with no additives.

Purity

Greater than 97.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
FGF22 is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities and are involved in a variety of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. The mouse homolog of this gene was found to be preferentially expressed in the inner root sheath of the hair follicle, which suggested a role in hair development.
Synonyms
Fibroblast growth factor 22, FGF-22.
Physical Appearance
Sterile Filtered white lyophilized powder.
Stability
Lyophilized Fibroblast Growth Factor 22 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-22 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Fibroblast Growth Factor-22 sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MTPSASRGPR SYPHLEGDVR WRRLFSSTHF FLRVDPGGRV QGTRWRHGQD SILEIRSVHV GVVVIKAVSS GFYVAMNRRG RLYGSRLYTV DCRFRERIEE NGHNTYASQR WRRRGQPMFL ALDRRGGPRP GGRTRRYHLS AHFLPVLVS.
Background
What is the molecular weight/Mw of FGF22 HUMAN Protein?
FGF22 HUMAN Protein has a total Mw of 17.3kDa.

What is the source or expression system of FGF22 HUMAN Protein?
Escherichia Coli.

What is the Purity of FGF22 HUMAN Protein?
FGF22 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF22 HUMAN Protein?
The biological functionality of FGF22 HUMAN Protein will be determined in the future.

What is the amino acid sequence of FGF22 HUMAN Protein?
MTPSASRGPR SYPHLEGDVR WRRLFSSTHF FLRVDPGGRV QGTRWRHGQD SILEIRSVHV GVVVIKAVSS GFYVAMNRRG RLYGSRLYTV DCRFRERIEE NGHNTYASQR WRRRGQPMFL ALDRRGGPRP GGRTRRYHLS AHFLPVLVS.

What applications can FGF22 HUMAN Protein be used in?
FGF22 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF22 HUMAN Protein?
The endotoxin level is minimal, FGF22 HUMAN Protein was purified using conventional chromatography techniques.

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

Description:

Small EDRK-Rich Factor 2 Human Recombinant

Small EDRK-rich factor 2, Gastric cancer-related protein VRG107, Protein 4F5-related, 4F5re, h4F5rel, FAM2C, HsT17089.

Product # :

PRO-1730

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Description

SERF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 82 amino acids (1-59 a.a) and having a molecular mass of 9.3kDa.SERF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SERF2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 30% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
SERF2 (small EDRK-rich factor 2) is a member of the SERF family. SERF2 is a protein-coding gene. Among the diseases associated with SERF2 are spinal muscular atrophy, and muscular atrophy.
Synonyms
Small EDRK-rich factor 2, Gastric cancer-related protein VRG107, Protein 4F5-related, 4F5re, h4F5rel, FAM2C, HsT17089.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMTRGNQR ELARQKNMKK QSDSVKGKRR DDGLSAAARK QRDSEIMQQK QKKANEKKEE PK

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

Description:

Keratinocyte Growth Factor Human Recombinant, Plant

HBGF-7, FGF7, FGF-7, KGF.

Product # :

CYT-1212

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Description

KGF Human Recombinant produced in Oryza Sativa is a single, polypeptide chain having a molecular mass of approximately 19.2kDa. The KGF is purified by proprietary chromatographic techniques.

Source

Rice Grain

Formulation

Lyophilized KGF from a 0.2μm filtered solution containing no stabilizers.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

KGF has full biological activity when compared to standards. The activity is determined by the dose-dependent proliferation of HUVECs and is typically 10ng/ml corresponding to a specific activity of 100,000U/mg.

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Introduction
KGF is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF7 is a potent epithelial cell-specific growth factor, whose mitogenic activity is predominantly exhibited in keratinocytes but not in fibroblasts and endothelial cells. Studies of mouse and rat homologs of this gene implicated roles in morphogenesis of epithelium, reepithelialization of wounds, hair development and early lung organogenesis.
Synonyms
HBGF-7, FGF7, FGF-7, KGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized KGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF7 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized KGF in sterile 18MΩ-cm at 100µg/ml, which can then be further diluted to other aqueous solutions.

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

Description:

B-cell Activating Factor Receptor Human Recombinant

TNFRSF13C, CD268, BAFF-R, MGC138235, B cell-activating factor receptor.

Product # :

CYT-429

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Description

B Lymphocyte Stimulator Receptor Human Recombinant extracellular produced in E.Coli is a single, non-glycosylated polypeptide chain containing 76 amino acids and having a molecular mass of 7.7 kDa.The BAFF-R is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated (1.0mg/ml) solution in 20mM PB, pH 8.0, 500mM NaCl.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Determined by its ability to block BAFF induced mouse splenocyte survival. The expected ED₅₀ for this effect is 1.0-5.0 µg/ml in the presence of 1.0µg/ml of human soluble BAFF.

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Introduction
B cell-activating factor (BAFF) enhances B-cell survival in vitro and is a regulator of the peripheral B-cell population. Overexpression of Baff in mice results in mature B-cell hyperplasia and symptoms of systemic lupus erythematosus (SLE). Also, some SLE patients have increased levels of BAFF in serum. Therefore, it has been proposed that abnormally high levels of BAFF may contribute to the pathogenesis of autoimmune diseases by enhancing the survival of autoreactive B cells. The protein encoded by this gene is a receptor for BAFF and is a type III transmembrane protein containing a single extracellular cysteine-rich domain. It is thought that this receptor is the principal receptor required for BAFF-mediated mature B-cell survival.
Synonyms
TNFRSF13C, CD268, BAFF-R, MGC138235, B cell-activating factor receptor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BAFF-R although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution B Lymphocyte Stimulator Receptor should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized B Lymphocyte Stimulator Receptor Recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MRRGPRSLRGRDAPAPTPCVPAECFDLLVRHCVACGLLRTPRPKPAG
ASSPAPRTALQPQESVGAGAGEAALPLPG.
Background
B-cell Activating Factor Receptor Human Recombinant: Unlocking the Potential of a Key Immunomodulatory Target
Abstract:
B-cell Activating Factor Receptor (BAFF-R) human recombinant is a critical component of the B-cell immune response, playing a pivotal role in B-cell survival, maturation, and antibody production. This research paper provides a comprehensive analysis of BAFF-R, including its characteristics, signaling pathways, and potential therapeutic applications. Furthermore, innovative methodologies for the production and optimization of BAFF-R human recombinant are proposed, shedding light on its future implications in the field of immunotherapy.
Introduction:
The immune system relies on the precise regulation of B-cell functions, with BAFF-R serving as a key modulator of B-cell development and activation. This paper explores the unique features of BAFF-R and presents novel approaches for its production and optimization, aiming to uncover its therapeutic potential.
Characteristics and Signaling Pathways:
BAFF-R is a type III transmembrane protein expressed primarily on B-cells. It belongs to the tumor necrosis factor receptor superfamily and binds specifically to B-cell activating factor (BAFF). Engagement of BAFF-R by BAFF initiates intracellular signaling cascades, including the activation of nuclear factor-kappa B (NF-κB) and mitogen-activated protein kinase (MAPK) pathways, promoting B-cell survival, proliferation, and differentiation.
Production of BAFF-R Human Recombinant:
Efficient production methodologies are crucial for the therapeutic application of BAFF-R human recombinant. Various expression systems, such as mammalian cell-based platforms, have been explored to ensure proper folding and post-translational modifications of the protein. Optimization strategies, including codon optimization and vector design, have been employed to enhance production efficiency. Purification techniques, such as affinity chromatography and size exclusion chromatography, have been optimized to isolate high-quality BAFF-R recombinant.
Potential Therapeutic Applications:
BAFF-R human recombinant holds great promise in the field of immunotherapy. Dysregulation of the BAFF/BAFF-R signaling axis has been implicated in autoimmune diseases, such as systemic lupus erythematosus and rheumatoid arthritis. Thus, modulating BAFF-R activity using BAFF-R human recombinant may provide a targeted therapeutic approach for these conditions. Additionally, BAFF-R represents a potential target for B-cell malignancies, and BAFF-R human recombinant may serve as an adjuvant therapy in combination with existing treatments.
Conclusion:
BAFF-R human recombinant represents a crucial immunomodulatory target with diverse therapeutic applications in immunotherapy. Optimizing production methodologies and further understanding its signaling pathways will enhance its clinical utility. With its potential implications in autoimmune diseases and B-cell malignancies, BAFF-R human recombinant holds immense promise as an innovative therapeutic tool for immune-related disorders.
What is the molecular weight/Mw of BAFF R Protein?
BAFF R Protein has a total Mw of 7.7kDa.

What is the source or expression system of BAFF R Protein?
Escherichia Coli.

What is the Purity of BAFF R Protein?
BAFF R Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BAFF R Protein?
Determined by its ability to block BAFF induced mouse splenocyte survival. The expected ED50 for this effect is 1.0-5.0 µg/ml in the presence of 1.0µg/ml of human soluble BAFF.

What is the amino acid sequence of BAFF R Protein?
MRRGPRSLRGRDAPAPTPCVPAECFDLLVRHCVACGLLRTPRPKPAG
ASSPAPRTALQPQESVGAGAGEAALPLPG.

What applications can BAFF R Protein be used in?
BAFF R Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BAFF R Protein?
The endotoxin level is minimal, BAFF R Protein was purified using conventional chromatography techniques.

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

Description:

Vascular Endothelial Growth Factor Receptor-1 Human Recombinant

FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

Product # :

PKA-240

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Description

Soluble FLT1 Human Recombinant produced in baculovirus is monomeric, glycosylated, polypeptide containing 687 amino acids and having a molecular mass of 96 kDa. The soluble receptor protein contains only the first 6 extracellular domains, which contain all the information necessary for binding of VEGF.The FLT1 is purified by proprietary chromatographic techniques.

Source

Insect Cells.

Formulation

FLT1 was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.

Purity

Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The activity of FLT1 was determined by its ability to inhibit the VEGF (165)-induced proliferation of HUVECs.

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Introduction
Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.
Synonyms
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FLT-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FLT1 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized FLT1 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SKLK DPELSLKGTQ HIMQAGQTLH LQCRGEAAHK WSLPEMVSKE SERLSITKSA CGRNGKQFCS TLTLNTAQAN HTGFYSCKYL AVPTSKKKET ESAIYIFISD TGRPFVEMYS EIPEIIHMTE GRELVIPCRV TSPNITVTLK KFPLDTLIPD GKRIIWDSRK GFIISNATYK EIGLLTCEAT VNGHLYKTNY LTHRQTNTII DVQISTPRPV KLLRGHTLVL NCTATTPLNT RVQMTWSYPD EKNKRASVRR RIDQSNSHAN IFYSVLTIDK MQNKDKGLYT CRVRSGPSFK SVNTSVHIYD KAFITVKHRK QQVLETVAGK RSYRLSMKVK AFPSPEVVWL KDGLPATEKS ARYLTRGYSL IIKDVTEEDA GNYTILLSIK QSNVFKNLTA TLIVNVKPQI YEKAVSSFPD PALYPLGSRQ ILTCTAYGIP QPTIKWFWHP CNHNHSEARC DFCSNNEESF ILDADSNMGN RIESITQRMA IIEGKNKMAS TLVVADSRIS GIYICIASNK VGTVGRNISF YITDVPNGFH VNLEKMPTEG EDLKLSCTVN KFLYRDVTWI LLRTVNNRTM HYSISKQKMA ITKEHSITLN LTIMNVSLQD SGTYACRARN VYTGEEILQK KEITIRGEHC NKKAVFSRIS KFKSTRNDCT TQSNVKH

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

Description:

Leukemia Inhibitory Factor Human Recombinant, Sf9

Leukemia Inhibitory Factor, Differentiation Inhibitory Activity, Cholinergic Differentiation Factor, Differentiation-Stimulating Factor, Hepatocyte-Stimulating Factor III, Differentiation-Inducing Factor, Melanoma-Derived LPL Inhibitor, Human Interleukin In DA Cells, D Factor, HILDA, MLPLI, Emfilermin, DIA, CDF, Leukemia inhibitory factor, LIF, Differentiation-stimulating factor, D factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin.

Product # :

CYT-1003

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Description

LIF Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 189 amino acids (23-202a.a.) and having a molecular mass of 20.8kDa (Molecular size on SDS-PAGE will appear at approximately 18-40kDa). LIF is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

LIF protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured in a cell proliferation assay using TF-1 human erythroleukemic cell. The ED50 for this effects is less or equal to 0.5 ng/ml.

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Introduction
Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.
Synonyms
Leukemia Inhibitory Factor, Differentiation Inhibitory Activity, Cholinergic Differentiation Factor, Differentiation-Stimulating Factor, Hepatocyte-Stimulating Factor III, Differentiation-Inducing Factor, Melanoma-Derived LPL Inhibitor, Human Interleukin In DA Cells, D Factor, HILDA, MLPLI, Emfilermin, DIA, CDF, Leukemia inhibitory factor, LIF, Differentiation-stimulating factor, D factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADPSPLPITP VNATCAIRHP CHNNLMNQIR SQLAQLNGSA NALFILYYTA QGEPFPNNLD KLCGPNVTDF PPFHANGTEK AKLVELYRIV VYLGTSLGNI TRDQKILNPS ALSLHSKLNA TADILRGLLS NVLCRLCSKY HVGHVDVTYG PDTSGKDVFQ KKKLGCQLLG KYKQIIAVLA
QAFHHHHHH.

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

Description:

Histidine NADH Dehydrogenase Fe-S Protein 2 Human Recombinant

CI-49 , NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial, Complex I-49kD, CI-49kD, NADH-ubiquinone oxidoreductase 49 kDa subunit, NDUFS2.

Product # :

ENZ-737

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Description

NDUFS2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (77-463a.a) and having a molecular mass of 46.5kDa. NDUFS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The NDUFS2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 80% as determined by SDS-PAGE.

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Introduction
NDUFS2 is a core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which is a part of the minimal assembly required for catalysis. Complex I takes part in the transfer of electrons from NADH to the respiratory chain. Histidine NADH Dehydrogenase Fe-S Protein 2 (NDUFS2) is required for catalytic activity. Imperfections in NDUFS2 are the source of complex I mitochondrial respiratory chain deficiency, which is characterized by many symptoms including liver failure, cardiomyopathy and neurodegeneration.
Synonyms
CI-49 , NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial, Complex I-49kD, CI-49kD, NADH-ubiquinone oxidoreductase 49 kDa subunit, NDUFS2.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSVKNITLN FGPQHPAAHG VLRLVMELSG EMVRKCDPHI GLLHRGTEKL IEYKTYLQAL PYFDRLDYVS MMCNEQAYSL AVEKLLNIRP PPRAQWIRVL FGEITRLLNH IMAVTTHALD LGAMTPFFWL FEEREKMFEF YERVSGARMH AAYIRPGGVH QDLPLGLMDD IYQFSKNFSL RLDELEELLT NNRIWRNRTI DIGVVTAEEA LNYGFSGVML RGSGIQWDLR KTQPYDVYDQ VEFDVPVGSR GDCYDRYLCR VEEMRQSLRI IAQCLNKMPP GEIKVDDAKV SPPKRAEMKT SMESLIHHFK LYTEGYQVPP GATYTAIEAP KGEFGVYLVS DGSSRPYRCK IKAPGFAHLA GLDKMSKGHM LADVVAIIGT QDIVFGEVDR.

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

Description:

OX40 Ligand Human Recombinant

Tumor necrosis factor ligand superfamily member 4, OX40 ligand, OX40L, OX-40L, CD252, Tnfsf4, Ox40l, Txgp1l, gp3, OX4, Ath-1, Ath1, CD134L, gp34, Tnlg2b, Txgp1l.

Product # :

CYT-1226

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Description

OX40L Human Recombinant is a single, glycosylated, polypeptide chain (51-183 a.a) containing a total of139 amino acids and having a molecular mass of 16.2 kDa. OX40L is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The OX40L solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured by its binding ability in a functional ELISA with Human OX40/TNFRSF4.

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Synonyms
Tumor necrosis factor ligand superfamily member 4, OX40 ligand, OX40L, OX-40L, CD252, Tnfsf4, Ox40l, Txgp1l, gp3, OX4, Ath-1, Ath1, CD134L, gp34, Tnlg2b, Txgp1l.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
QVSHRYPRIQ SIKVQFTEYK KEKGFILTSQ KEDEIMKVQN NSVIINCDGF YLISLKGYFS QEVNISLHYQ KDEEPLFQLK KVRSVNSLMV ASLTYKDKVY LNVTTDNTSL DDFHVNGGEL ILIHQNPGEF CVLHHHHHH.
Background
OX40 Ligand (OX40L), a member of the tumor necrosis factor (TNF) superfamily, plays a pivotal role in regulating immune responses and orchestrating the delicate balance between activation and tolerance. The human recombinant form of OX40L has emerged as a potent tool in immunology, offering insights into its molecular intricacies and potential applications in therapeutic interventions. This research embarks on a journey to unravel the multifaceted role of OX40L Human Recombinant, shedding light on its structural attributes, signaling pathways, and its promising avenues in immunotherapy. By delving into the properties of OX40L, scientists aim to expand our understanding of immune modulation and open new frontiers in the treatment of immune-related disorders.
Structural Insights into OX40L Human Recombinant:
OX40L, as a trimeric transmembrane protein, exhibits a unique structural configuration that governs its interactions with the OX40 receptor on T cells. The human recombinant form, engineered for controlled study, provides a window into the three-dimensional intricacies of the ligand. Understanding its structure is pivotal for deciphering how OX40L engages with its receptor and modulates immune responses.
Immunomodulatory Signaling Pathways:
OX40L binding to its cognate receptor OX40 on T cells triggers intricate signaling cascades that impact immune cell activation, proliferation, and cytokine production. The OX40-OX40L axis is a crucial regulator of T cell function, influencing both effector and regulatory T cell responses. Unraveling the specific pathways activated by OX40L Human Recombinant provides valuable insights into the modulation of immune responses in health and disease.
Applications in Immunotherapy:
The immunomodulatory properties of OX40L make it an attractive candidate for therapeutic interventions. OX40L Human Recombinant, in preclinical and clinical studies, is being explored for its potential in enhancing antitumor immune responses. By harnessing the ligand's ability to stimulate effector T cells and memory T cell formation, researchers aim to develop novel immunotherapies for cancer and other immune-related disorders.
OX40L in Autoimmune Diseases:
Conversely, OX40L's role in autoimmune diseases has spurred investigations into its inhibition as a therapeutic strategy. Blocking the OX40-OX40L interaction has shown promise in mitigating autoimmune responses, presenting a potential avenue for the development of treatments for conditions such as rheumatoid arthritis and inflammatory bowel disease.
While the potential of OX40L Human Recombinant in immunotherapy is promising, challenges persist. Fine-tuning its applications, understanding potential side effects, and optimizing dosages are critical considerations for translational success. Additionally, comprehending the context-dependent nature of OX40L signaling is essential for tailoring therapeutic strategies to specific diseases and patient profiles.
OX40L Human Recombinant stands at the forefront of immunomodulation research, offering a lens through which we can unravel the complexities of immune responses. Its structural insights, signaling pathways, and therapeutic applications position it as a key player in the evolving landscape of immunotherapy. As researchers continue to dissect the molecular nuances of OX40L, they not only expand our understanding of immune regulation but also pave the way for transformative advancements in the treatment of cancer and autoimmune diseases, shaping the future of precision medicine and immunotherapy.

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

Description:

Beta-Nerve Growth Factor Mouse

Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

Product # :

CYT-440

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Description

NGF beta Mouse produced in Submaxillary Gland of Grown Mouse is a homodimer, non-glycosylated, polypeptide chain containing 2 identical 120 amino acids and having a molecular mass of 13,471 Dalton each.The NGF beta Mouse is purified by advanced biology purification technology.

Source

Submaxillary Gland of Grown Mouse.

Formulation

The NGF beta Mouse was lyophilized from solution containing 5% mannitol and 1% HSA.

Purity

Greater than 98% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE .

Biological Activity

The method used to test the bioassay is the NGF-dependent survival of dorsal root ganglia neurons of chick embryo, corresponding to a Specific Activity of 500,000IU/mg.

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Introduction
NGF-beta has nerve growth stimulating activity and the complex is involved in the regulation of growth and the differentiation of sympathetic and certain sensory neurons. Mutations in this gene have been associated with hereditary sensory and autonomic neuropathy, type 5 (HSAN5), and dysregulation of this gene's expression is associated with allergic rhinitis.
Synonyms
Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Mouse Beta-NGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Murine NGF-Beta should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Murine NGF-beta in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SSTHPVFHMGEF SVCDSVSVWV GDKTTATDIK GKEVTVLAEV NINNSVFRQY FFETKCRASN PVESGCRGID SKHWNSYCTT THTFVKALTT DEKQAAWRFI RIDTACVCVL SRKATRRG.
Background
What is the molecular weight/Mw of B NGF Protein?
B NGF Protein has a total Mw of 13kDa.

What is the source or expression system of B NGF Protein?
Submaxillary Gland of Grown Mouse.

What is the Purity of B NGF Protein?
B NGF Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of B NGF Protein?
The method used to test the bioassay is the NGF-dependent survival of dorsal root ganglia neurons of chick embryo, corresponding to a Specific Activity of 500,000IU/mg.

What is the amino acid sequence of B NGF Protein?
SSTHPVFHMGEF SVCDSVSVWV GDKTTATDIK GKEVTVLAEV NINNSVFRQY FFETKCRASN PVESGCRGID SKHWNSYCTT THTFVKALTT DEKQAAWRFI RIDTACVCVL SRKATRRG.

What applications can B NGF Protein be used in?
B NGF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for XXX Protein?
The endotoxin level is minimal, XXX Protein was purified using conventional chromatography techniques.

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

Description:

Macrophage Colony Stimulating Factor Rat Recombinant HEK

CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.

Product # :

CYT-046

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Description

MCSF Rat Recombinant produced in HEK-293 cells is a secreted protein (amino acids Glu33-Arg254). M-CSF is disulfide-linked homodimer containing 2 x 222 a.a chains.

Source

HEK293

Formulation

The recombinant MCSF was lyophilized after extensive dialysis against PBS.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50 of 3-4ng/ml is measured by its ability to stimulate the proliferation of mouse M-NFS-60 cells.

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Introduction
Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. CSF-1 induces cells of the monocyte/macrophage lineage. It plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.
Synonyms
CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the MCSF in sterile PBS not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

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

Description:

Ciliary Neurotrophic Factor Rat Recombinant, His Tag

Ciliary neurotrophic factor, CNTF, Cntf.

Product # :

CYT-926

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Description

CNTF Rat Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 223 amino acids (1-200a.a) and having a molecular mass of 25.2kDa.CNTF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CNTF protein solution (0.5mg/ml) containing phosphate buffered saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy.
Synonyms
Ciliary neurotrophic factor, CNTF, Cntf.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAFAEQT PLTLHRRDLC SRSIWLARKI RSDLTALMES YVKHQGLNKN INLDSVDGVP VASTDRWSEM TEAERLQENL QAYRTFQGML TKLLEDQRVH FTPTEGDFHQ AIHTLMLQVS AFAYQLEELM VLLEQKIPEN EADGMPATVG DGGLFEKKLW GLKVLQELSQ WTVRSIHDLR VISSHQMGIS ALESHYGAKD KQM.
Background
What is the molecular weight/Mw of CNTF Protein?
CNTF Protein has a total Mw of 25.2kDa.

What is the source or expression system of CNTF Protein?
Escherichia Coli.

What is the Purity of CNTF Protein?
CNTF Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CNTF Protein?
The biological functionality of CNTF Protein will be determined in the future.

What is the amino acid sequence of CNTF Protein?
MGSSHHHHHH SSGLVPRGSH MGSMAFAEQT PLTLHRRDLC SRSIWLARKI RSDLTALMES YVKHQGLNKN INLDSVDGVP VASTDRWSEM TEAERLQENL QAYRTFQGML TKLLEDQRVH FTPTEGDFHQ AIHTLMLQVS AFAYQLEELM VLLEQKIPEN EADGMPATVG DGGLFEKKLW GLKVLQELSQ WTVRSIHDLR VISSHQMGIS ALESHYGAKD KQM.
What applications can CNTF Protein be used in?
CNTF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CNTF Protein?
The endotoxin level is minimal, CNTF Protein was purified using conventional chromatography techniques

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

Description:

Canopy 3 Homolog Human Recombinant

CAG4A, ERDA5, PRAT4A, TNRC5, Protein canopy homolog 3, CTG repeat protein 4a, Expanded repeat-domain protein CAG/CTG 5, Protein associated with TLR4, Trinucleotide repeat-containing gene 5 protein,CNPY3.

Product # :

PRO-1386

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Description

CNPY3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 271 amino acids (31-278 a.a.) and having a molecular mass of 29.9kDa. CNPY3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

CNPY3 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Canopy 3 homolog (CNPY3) is a 271 a.aToll-like receptor specific co-chaperone for HSP90B1. CNPY3 is necessitated for proper TLR folding, excluding that of TLR3, and so controls TLR exit from the endoplasmic reticulum. Therefore, CNPY3i s required for both innate and adaptive immune responses.
Synonyms
CAG4A, ERDA5, PRAT4A, TNRC5, Protein canopy homolog 3, CTG repeat protein 4a, Expanded repeat-domain protein CAG/CTG 5, Protein associated with TLR4, Trinucleotide repeat-containing gene 5 protein,CNPY3.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSGPSQAGA EENDWVRLPS KCEVCKYVAV ELKSAFEETG KTKEVIGTGY GILDQKASGV KYTKSDLRLI EVTETICKRL LDYSLHKERT GSNRFAKGMS ETFETLHNLV HKGVKVVMDI PYELWNETSA EVADLKKQCD VLVEEFEEVI EDWYRNHQEE DLTEFLCANH VLKGKDTSCL AEQWSGKKGD TAALGGKKSK KKSSRAKAAG GRSSSSKQRK ELGGLEGDPS PEEDEGIQKA SPLTHSPPDE L.

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

Description:

Fibroblast Growth Factor Receptor 4 Fc Chimera Human Recombinant

Fibroblast Growth Factor Receptor 4, EC 2.7.10.1, JTK2, TKF, Tyrosine Kinase Related To Fibroblast Growth Factor Receptor, Hydroxyaryl-Protein Kinase, Protein-Tyrosine Kinase, Tyrosylprotein Kinase, CD334 Antigen, EC 2.7.10, FGFR-4, CD334, FGFR4.

Product # :

PKA-233

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Description

Soluble FGFR-4a (IIIc) Fc Chimera Human Recombinant fused with Xa cleavage site with the Fc part of human IgG1 produced in baculovirus is a heterodimeric, glycosylated, Polypeptide chain and having a molecular mass of 170 kDa. The FGFR4 is purified by proprietary chromatographic techniques.

Source

Insect Cells.

Formulation

CD334 was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.

Purity

Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Determined by its ability to inhibit human FGF acidic-dependent proliferation on R1 cells. The ED50 for this effect is typically at 15.0-30.0 ng/ml.

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Introduction
Fibroblast growth factors (FGFs) comprise a family of at least eighteen structurally related proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentiation, angiogenesis, wound healing and tumorgenesis. The biological activities of the FGFs are mediated by a family of type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Four distinct genes encoding closely related FGF receptors, FGF R1 - 4, are known. All four genes for FGF Rs encode proteins with an N-terminal signal peptide, three immunoglobulin (Ig)-like domains, an acid-box region containing a run of acidic residues between the IgI and IgII domains, a transmembrane domain and the split tyrosine-kinase domain. Multiple forms of FGF R1 - 3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGF R1 and 2 results in receptors containing all three Ig domains, referred to as the a isoform, or only IgII and IgIII, referred to as the b isoform. Only the a isoform has been identified for FGF R3 and FGF R4. Additional splicing events for FGF R1 - 3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGF R1. Mutations in FGF R1 - 3 have been found in patients with birth defects involving craniosynostosis. The complex patterns of expression of these receptors as well as the specificity of their interactions with the various FGF ligand family members are under investigation.
Synonyms
Fibroblast Growth Factor Receptor 4, EC 2.7.10.1, JTK2, TKF, Tyrosine Kinase Related To Fibroblast Growth Factor Receptor, Hydroxyaryl-Protein Kinase, Protein-Tyrosine Kinase, Tyrosylprotein Kinase, CD334 Antigen, EC 2.7.10, FGFR-4, CD334, FGFR4.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGFR4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGFR4 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized FGFR-4 in sterile PBS not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

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

Description:

Macrophage-Colony Stimulating Factor Mouse Recombinant

CSF-1, Lanimostim, MCSF, M-CSF.

Product # :

CYT-439

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Quantity :

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Shipped at Room temp

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Description

Macrophage Colony Stimulating Factor Mouse Recombinant produced in E.coli is a disulfide linked homodimer, non-glycosylated, polypeptide chain containing 2 x 156 amino acids and having a total molecular mass of 36.4 KD.MCSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a sterile (0.2µm) filtered solution containing 10mM sodium phosphate, 50mM sodium chloride, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as calculated by the dose-dependant stimulation of the proliferation of murine M-NFS-60 indicator cells is 1.33ng/ml corresponding to a specific activity of 7.5x10⁵ units/mg.

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Introduction
Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. CSF-1 induces cells of the monocyte/macrophage lineage. It plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.
Synonyms
CSF-1, Lanimostim, MCSF, M-CSF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized M-CSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized M-CSF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MKEVSEHCSH MIGNGHLKVL QQLIDSQMET SCQIAFEFVD QEQLDDPVCY LKKAFFLVQD IIDETMRFKD NTPNANATER LQELSNNLNS CFTKDYEEQN KACVRTFHET PLQLLEKIKN FFNETKNLLE KDWNIFTKNC NNSFAKCSSR DVVTKP.
Background
Macrophage-Colony Stimulating Factor Mouse Recombinant: An In-Depth Analysis
Abstract:
Macrophage-Colony Stimulating Factor (M-CSF) is a crucial cytokine involved in the regulation of macrophage biology, including their differentiation, survival, and function. This research paper provides an in-depth analysis of M-CSF Mouse Recombinant, focusing on its structure, signaling pathways, and diverse functions in the context of human research. Additionally, the paper explores the therapeutic potential of M-CSF modulation in various diseases.
Introduction:
M-CSF plays a vital role in the development and maintenance of macrophages, key immune cells involved in innate immunity and tissue homeostasis. This paper aims to provide a comprehensive analysis of M-CSF Mouse Recombinant, highlighting its importance in human macrophage biology and its potential therapeutic applications.
Structure and Function of M-CSF:
M-CSF is a homodimeric protein that binds to its receptor, CSF-1R, leading to the activation of downstream signaling pathways. It regulates the proliferation, survival, and activation of macrophages, influencing immune responses and tissue remodeling processes.
Signaling Pathways:
Upon binding to CSF-1R, M-CSF triggers various intracellular signaling pathways, including the MAPK pathway, PI3K/Akt pathway, and JAK/STAT pathway. These pathways regulate gene expression and mediate cellular responses, impacting macrophage functions.
Role in Macrophage Development and Function:
M-CSF is essential for the differentiation and maturation of macrophages from hematopoietic progenitor cells. It promotes the survival, proliferation, and activation of macrophages, enhancing their phagocytic activity, cytokine production, and antigen presentation capabilities.
Therapeutic Potential:
Given its crucial role in macrophage biology, M-CSF modulation has emerged as a potential therapeutic strategy. M-CSF inhibitors and CSF-1R antagonists have shown promise in the treatment of inflammatory and autoimmune diseases, as well as certain cancers. Targeting M-CSF signaling can modulate immune responses and affect disease progression.
Clinical Applications and Future Directions:
The therapeutic potential of M-CSF modulation is being explored in various clinical settings. Clinical trials investigating M-CSF inhibitors as monotherapy or combination therapy are underway in diseases such as rheumatoid arthritis and cancer. Future research should focus on understanding the intricate mechanisms of M-CSF signaling, optimizing therapeutic strategies, and developing personalized treatment approaches.

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

Description:

TMEFF1 Human Recombinant

C9orf2, CT120.1, H7365, TR-1, Tomoregulin-1, Transmembrane protein with EGF-like and one follistatin-like domain, TMEFF1.

Product # :

PRO-1429

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source
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Description

TMEFF1 Human Recombinant produced in E. coli is a single polypeptide chain containing 314 amino acids (40-330) and having a molecular mass of 33.9kDa. TMEFF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The TMEFF1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
TMEFF1 is a type I transmembrane glycoprotein which includes 2 follistatin modules and an EGF domain in its extracellular domain, a transmembrane domain and a short cytoplasmic tail. The extracellular domain of TMEFF1 can be released as a soluble protein. TMEFF1 is primarily expressed in brain, but is downregulated in brain neoplasms. TMEFF1 selectively regulates nodal but not activin signaling through direct binding to the nodal co-receptor, Cripto. TMEFF inhibits NODAL and BMP signaling through neural patterning and also a possible tumor suppressor in brain cancers.
Synonyms
C9orf2, CT120.1, H7365, TR-1, Tomoregulin-1, Transmembrane protein with EGF-like and one follistatin-like domain, TMEFF1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSNQPPGG GGGSGGDCPG GKGKSINCSE LNVRESDVRV CDESSCKYGG VCKEDGDGLK CACQFQCHTN YIPVCGSNGD TYQNECFLRR AACKHQKEIT VIARGPCYSD NGSGSGEGEE EGSGAEVHRK HSKCGPCKYK AECDEDAENV GCVCNIDCSG YSFNPVCASD GSSYNNPCFV REASCIKQEQ IDIRHLGHCT DTDDTSLLGK KDDGLQYRPD VKDASDQRED VYIGNHMPCP ENLNGYCIHG KCEFIYSTQK ASCRCESGYT GQHCEKTDFS ILYVVPSRQK LTHV.

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

Description:

Family with Sequence Similarity 3, Member D Human Recombinant

Protein FAM3D, FAM3D, EF7, OIT1.

Product # :

PRO-1585

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Description

FAM3D Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 26-224) containing 209 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 23.3kDa (calculated).

Source

Escherichia Coli.

Formulation

FAM3D filtered (0.4 µm) and lyophilized from 0.5mg/ml in 0.05M Acetate buffer pH-4.0.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Family with Sequence Similarity 3, Member D (FAM3D) is a member of the FAM3 family. The FAM3D gene is linked to narcolepsy and diabetes mellitus in pancreatic adenocarcinoma, however FAM3D function of remains vague. FAM3D is amply expressed in the placenta and weakly expressed in the small intestine.
Synonyms
Protein FAM3D, FAM3D, EF7, OIT1.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely at 37°C. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. FAM3D is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHASYMSFSMKTIR LPRWLAASPT KEIQVKKYKC GLIKPCPANY FAFKICSGAA NVVGPTMCFE DRMIMSPVKN NVGRGLNIAL VNGTTGAVLG QKAFDMYSGD VMHLVKFLKE IPGGALVLVA SYDDPGTKMN DESRKLFSDL GSSYAKQLGF RDSWVFIGAK DLRGKSPFEQ FLKNSPDTNK YEGWPELLEM EGCMPPKPF.

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

Description:

Platelet-Derived Growth Factor B Human Recombinant

Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.

Product # :

CYT-492

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Description

PDGF-B Human Recombinant mature chain produced in E.Coli is a non-glycosylated, polypeptide chain containing 109 amino acids fragment (82-190) and having a molecular mass of 16.75 kDa. The PDGF-B is fused with an amino-terminal hexahistidine tag and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Platelet-Derived Growth Factor-B is supplied in 25mM Na-Acetate pH 4.8, 1mM EDTA and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
The term ‘PDGF’ refers to a family of disulphide bond-linked dimeric isoforms that act as autocrine and paracrine growth factors and are produced by a variety of cell types other than platelets.
They act as potent mitogens for almost all mesenchymally-derived cells. Aberrant expression is involved in certain cancers, fibroproliferative disorders and atherosclerosis. The protein also contributes to wound healing and neural regeneration. There are four members of the PDGF family – PDGF A, PDGF B, PDGF C and PDGF D. Two distinct types of PDGF-A exist – a short form that is soluble and a long form that is retained by the extracellular matrix.
Synonyms
Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.

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

Description:

Fibroblast Growth Factor 12 Human Recombinant

FGF-12, FGF12, FGF12B, FHF1, Fibroblast growth factor 12, Fibroblast growth factor homologous factor 1, FHF-1, Myocyte-activating factor.

Product # :

CYT-1113

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Description

Fibroblast Growth Factor 12 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 181 amino acids and having a molecular mass of 20.5kDa. The FGF12 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4 and 1mM DTT.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Determined by FGF12 binding ability in a functional ELISA. Immobilized FGFR4/Fc Chimera at 5 µg/mL (100 µL/well) can bind FGF12 with a linear range of 1.6100 ng/mL.

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Introduction
FGF12 is part of the Fibroblast Growth Factor (FGF) family which has a vast mitogenic and cell survival functions, and play a role in a range of biological activities, among them are embryonic development, cell growth, morphogenesis, tissue repair, tumor growth, and invasion. FGF-12 doesn’t obtain the N-terminal signal sequence present in the majority of the FGF family members, but it contains clusters of basic residues that act as a nuclear localization signal. When transfected into mammalian cells, FGF12 accumulated in the nucleus, but was not secreted. FGF12 is involved in nervous system development and function. FGF12 binds to IB2 (islet brain-2), a cellular kinase scaffold, and voltage gated sodium channels and is also involved in intracellular signalling and ion exchange.
Synonyms
FGF-12, FGF12, FGF12B, FHF1, Fibroblast growth factor 12, Fibroblast growth factor homologous factor 1, FHF-1, Myocyte-activating factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF12 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor 12 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Fibroblast Growth Factor 12 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MESKEPQLKG IVTRLFSQQG YFLQMHPDGT IDGTKDENSD YTLFNLIPVG LRVVAIQGVK ASLYVAMNGE GYLYSSDVFT PECKFKESVF ENYYVIYSST LYRQQESGRA WFLGLNKEGQ IMKGNRVKKT KPSSHFVPKP IEVCMYREQS LHEIGEKQGR SRKSSGTPTM NGGKVVNQDS T.
Background
What is the molecular weight/Mw of FGF12 Protein?
FGF12 Protein has a total Mw of 20.5kDa.

What is the source or expression system of FGF12 Protein?
Escherichia Coli.

What is the Purity of FGF12 Protein?
FGF12 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF12 Protein?
Determined by FGF12 binding ability in a functional ELISA. Immobilized FGFR4/Fc Chimera at 5 µg/mL (100 µL/well) can bind FGF12 with a linear range of 1.6100 ng/mL.

What is the amino acid sequence of FGF12 Protein?
MESKEPQLKG IVTRLFSQQG YFLQMHPDGT IDGTKDENSD YTLFNLIPVG LRVVAIQGVK ASLYVAMNGE GYLYSSDVFT PECKFKESVF ENYYVIYSST LYRQQESGRA WFLGLNKEGQ IMKGNRVKKT KPSSHFVPKP IEVCMYREQS LHEIGEKQGR SRKSSGTPTM NGGKVVNQDS T.

What applications can FGF12 Protein be used in?
FGF12 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF12 Protein?
The endotoxin level is minimal, FGF12 Protein was purified using conventional chromatography techniques.

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

Description:

Glia Maturation Factor Beta Mouse Recombinant

Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF, C79176, AI851627, D14Ertd630e, 3110001H22Rik, 3110001O16Rik.

Product # :

CYT-006

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Description

Glia Maturation Factor-Beta (GMF-Beta) Mouse Recombinant produced in E.Coli is a signle, non-glycosylated, polypeptide chain containing 141 amino acids and having a total molecular mass of 16.6kDa. GMF-Beta, Mouse Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GMF-beta protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

More Info

Introduction
GMFB is part of the GMF subfamily of the larger actin-binding protein ADF family. GMFB is phosphorylated after phorbol ester stimulation, and is crucial for the nervous system. GMFB causes brain cell differentiation, stimulates neural regeneration and inhibits tumor cell proliferation. GMFB overexpression in astrocytes results in the increase of BDNF production. GMFB expression is increased by exercise, thus BDNF is important for exercise-induction of BDNF.
Synonyms
Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF, C79176, AI851627, D14Ertd630e, 3110001H22Rik, 3110001O16Rik.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GMF-B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMF-beta should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized GMFB in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SESLVVCDVA EDLVEKLRKF RFRKETHNAA IIMKIDKDER LVVLDEELEG
VSPDELKDEL PERQPRFIVY SYKYQHDDGR VSYPLCFIFS SPVGCKPEQQ
MMYAGSKNKL VQTAELTKVF EIRNTEDLTE EWLREKLGFF H.
Background
What is the molecular weight/Mw of GMFB MOUSE Protein?
GMFB MOUSE Protein has a total Mw of 16.6kDa.

What is the source or expression system of GMFB MOUSE Protein?
Escherichia Coli.

What is the Purity of GMFB MOUSE Protein?
GMFB MOUSE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of GMFB MOUSE Protein?
The biological functionality of GMFB MOUSE Protein will be determined in the future.

What is the amino acid sequence of GMFB MOUSE Protein?
SESLVVCDVA EDLVEKLRKF RFRKETHNAA IIMKIDKDER LVVLDEELEG
VSPDELKDEL PERQPRFIVY SYKYQHDDGR VSYPLCFIFS SPVGCKPEQQ
MMYAGSKNKL VQTAELTKVF EIRNTEDLTE EWLREKLGFF H.

What applications can GMFB MOUSE Protein be used in?
GMFB MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GMFB MOUSE Protein?
The endotoxin level is minimal, GMFB MOUSE Protein was purified using conventional chromatography techniques.

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

Description:

MTHFD2 Human Recombinant

Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial, NAD-dependent methylenetetrahydrofolate dehydrogenase, Methenyltetrahydrofolate cyclohydrolase, NMDMC, MTHFD2.

Product # :

ENZ-853

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Description

MTHFD2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (30-350) and having a molecular mass of 37.2kDa.MTHFD2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MTHFD2 solution (1mg/ml) contains Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
MTHFD2 plays a role as a homodimer which requires magnesium and inorganic phosphate. MTHFD2 has a pseudogene on chromosome 7 and owns 3 different enzymatic activities. Each of the activities catalyzes 1 of 3 sequential reactions in the interconversion of 1-carbon derivatives of tetrahydrofolate, which are substrates for methionine, thymidylate, and de novo purine syntheses.
Synonyms
Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial, NAD-dependent methylenetetrahydrofolate dehydrogenase, Methenyltetrahydrofolate cyclohydrolase, NMDMC, MTHFD2.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSLAAVRNE AVVISGRKLA QQIKQEVRQE VEEWVASGNK RPHLSVILVG ENPASHSYVL NKTRAAAVVG INSETIMKPA SISEEELLNL INKLNNDDNV DGLLVQLPLP EHIDERRICN AVSPDKDVDG FHVINVGRMC LDQYSMLPAT PWGVWEIIKR TGIPTLGKNV VVAGRSKNVG MPIAMLLHTD GAHERPGGDA TVTISHRYTP KEQLKKHTIL ADIVISAAGI PNLITADMIK EGAAVIDVGI NRVHDPVTAK PKLVGDVDFE GVRQKAGYIT PVPGGVGPMT VAMLMKNTII AAKKVLRLEE REVLKSKELG VATN.

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

Description:

Heat Shock Transcription Factor, Y-Linked 1 Human Recombinant

Heat shock transcription factor, Y-linked, Heat shock transcription factor 2-like protein, HSF2-like, HSFY1, HSF2L, HSFY, HSFY2, Y-linked isoform 1, Y-Linked 1.

Product # :

HSP-059

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Description

HSFY1 Human Recombinant produced in E. coli is a single polypeptide chain containing 424 amino acids (1-401) and having a molecular mass of 47.5kDa.HSFY1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The HSFY1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 80.0% as determined by SDS-PAGE.

More Info

Introduction
Heat Shock Transcription Factor, Y-Linked 1 (HSFY1) is a member of the heat shock factor (HSF) family of transcriptional activators for heat shock proteins. HSFY1 is localizes to an area of chromosome Y which is from time to time deleted in infertile males and therefore is considered a gene for azoospermia. The genome has 2 identical duplicates of HSFY1 within a palindromic area.
Synonyms
Heat shock transcription factor, Y-linked, Heat shock transcription factor 2-like protein, HSF2-like, HSFY1, HSF2L, HSFY, HSFY2, Y-linked isoform 1, Y-Linked 1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAHVSSE TQDVSPKDEL TASEASTRSP LCEHTFPGDS DLRSMIEEHA FQVLSQGSLL ESPSYTVCVS EPDKDDDFLS LNFPRKLWKI VESDQFKSIS WDENGTCIVI NEELFKKEIL ETKAPYRIFQ TDAIKSFVRQ LNLYGFSKIQ QNFQRSAFLA TFLSEEKESS VLSKLKFYYN PNFKRGYPQL LVRVKRRIGV KNASPISTLF NEDFNKKHFR AGANMENHNS ALAAEASEES LFSASKNLNM PLTRESSVRQ IIANSSVPIR SGFPPPSPST SVGPSEQIAT DQHAILNQLT TIHMHSHSTY MQARGHIVNF ITTTTSQYHI ISPLQNGYFG LTVEPSAVPT RYPLVSVNEA PYRNMLPAGN PWLQMPTIAD RSAAPHSRLA LQPSPLDKYH PNYN.

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

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