Search: 919 results found for "Mitochondrial Transcription Factor"

Description:

Testis Derived Transcript Human Recombinant

TESS, TESS-2, Testin.

Product # :

PRO-549

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

TES Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 441amino acids (1-421 a.a.) and having a molecular mass of 50.1 kDa. The TES protein is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TES 0.5mg/ml protein solution contains 20mM Tris pH-8, 1mM DTT, 0.1M NaCl & 20% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
TES also called Testin is a tumor suppressor protein which is involved in cell adhesion, cell spreading and in the restructuring of the actin cytoskeleton. TES protein localizes to cell-cell contacts and actin stress fibres, and interacts with a diversity of cytoskeletal proteins such as Zyxin, Mena, VASP, Talin and Actin. The ability of TES to associate with alpha-actinin, paxillin and Zyxin is dependent on the conformational form of the protein.
Synonyms
TESS, TESS-2, Testin.
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 MDLENKVKKM GLGHEQGFGA PCLKCKEKCE GFELHFWRKI CRNCKCGQEE HDVLLSNEED RKVGKLFEDT KYTTLIAKLK SDGIPMYKRN VMILTNPVAA KKNVSINTVT YEWAPPVQNQ ALARQYMQML PKEKQPVAGS EGAQYRKKQL AKQLPAHDQD PSKCHELSPR EVKEMEQFVK KYKSEALGVG DVKLPCEMDA QGPKQMNIPG GDRSTPAAVG AMEDKSAEHK RTQYSCYCCK LSMKEGDPAI YAERAGYDKL WHPACFVCST CHELLVDMIY FWKNEKLYCG RHYCDSEKPR CAGCDELIFS NEYTQAENQN WHLKHFCCFD CDSILAGEIY VMVNDKPVCK PCYVKNHAVV CQGCHNAIDP EVQRVTYNNF SWHASTECFL CSCCSKCLIG QKFMPVEGMV FCSVECKKRM S.

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 Factor-4 Human (CXCL4)

CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

Product # :

CHM-234

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info
Citations

Description

Human PF-4 a 7.8 kDa protein consisting of 70 amino acid residues.

Source

Human Platelets.

Formulation

The CXCL4 protein was lyophilized in PBS buffer pH-7.4.

Purity

Greater than 98.0% as determined by SDS-PAGE.

More Info

Introduction
Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets and binds with high affinity to heparin. Its major physiologic role appears to be neutralization of heparin-like molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemokine family. Human PF4 is used for the proof of heparin-induced thrombocytopenia. Furthermore it is used as an inhibitor in the angiogenesis during tumor therapy.
Synonyms
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
Physical Appearance
Sterile Filtered white lyophilized powder.
Stability
Human CXCL4 although stable at 25°C 1 week, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized CXCL4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first four N-terminal amino acids was determined and was found to be Glu-Ala-Glu-Glu.
Background
What is the molecular weight/Mw of CXCL4 Protein?
CXCL4 Protein has a total Mw of 7.8kDa.

What is the source or expression system of CXCL4 Protein?
Human Platelets.

What is the Purity of CXCL4 Protein?
CXCL4 Protein is > 98% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL4 Protein?
The biological functionality of CXCL4 Protein will be determined in the future.

What is the amino acid sequence of CXCL4 Protein?
The sequence of the first four N-terminal amino acids was determined and was found to be Glu-Ala-Glu-Glu.

What applications can CXCL4 Protein be used in?
CXCL4 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL4 Protein?
The endotoxin level is minimal, CXCL4 Protein was purified using conventional chromatography techniques.

Who supplies CXCL4 that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CXCL4?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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:

ADP-Ribosylation Factor-Like 1 Human Recombinant

ARFL1.

Product # :

PRO-508

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

ARL1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-181 a.a.) and having a molecular mass of 22.5 kDa. The ARL1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The ARL1 solution (0.25mg/ml) containing 20mM Tris-HCl pH-8, 2mM DTT, 100mM NaCl and 40% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
ARL1 is part of the ARL (ADP-ribosylation factor-like) family of proteins, which are structurally associated to ADP-ribosylation factors (ARFs). ARFs, described as activators of cholera toxin (CT) ADP-ribosyltransferase activity, control intracellular vesicular membrane trafficking, and stimulate a phospholipase D (PLD) isoform.
ARL1 is a weak stimulator of PLD and CT in a phospholipid dependent manner.
ARL1 is a GTP-binding protein that has low efficiency as allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. ARL1 is involved in the Golgi apparatus.
Synonyms
ARFL1.
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 MGGFFSSIFS SLFGTREMRI LILGLDGAGK TTILYRLQVG EVVTTIPTIG FNVETVTYKN LKFQVWDLGG QTSIRPYWRC YYSNTDAVIY VVDSCDRDRI GISKSELVAM LEEEELRKAI LVVFANKQDM EQAMTSSEMA NSLGLPALKD RKWQIFKTSA TKGTGLDEAM EWLVETLKSR Q.

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:

Glutathione Reductase, Mouse Anti Human

Glutathione reductase mitochondrial, GR, GRase, GSR, GLUR, GRD1.

Product # :

ANT-549

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

formulation
More Info
Citations

Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

More Info

Introduction
Glutathione reductase (GSR) belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. The GSR enzyme is a homodimeric flavoprotein and has a role in maintaining glutathione (GSH) in its reduced form by catalyzing the reduction of glutathione disulfide (GSSG): GSSG + NADPH + H+ ->2GSH + NADP+. In the majority of eukaryotic cells, GSR upholds the ratio of [GSH] / [GSSG], and partakes in quite a few critical functions such as the detoxification of reactive oxygen species as well as protein and DNA biosynthesis.
Synonyms
Glutathione reductase mitochondrial, GR, GRase, GSR, GLUR, GRD1.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human GSR mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human GSR amino acids 43-522 purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and k light chain.
Clone
PAT11D10AT.
Applications
GSR antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:500.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
GSR antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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:

Endocrine Gland Vascular Endothelial Growth Factor Mouse Recombinant

PK1, Prokineticin 1, EG-VEGF, Prok1, Endocrine-gland-derived vascular endothelial growth factor.

Product # :

CYT-825

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info
Citations

Description

EG-VEGF Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids and having a molecular mass of 9.6kDa.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS pH7.4 and 3% Trehalose.

Purity

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

More Info

Introduction
Endocrine gland-derived vascular endothelial growth factor (EG-VEGF) induces proliferation, migration, and fenestration in capillary endothelial cells derived from endocrine glands. Its expression is induced by hypoxia and is restricted to the steroidogenic glands (ovary, testis, adrenal, and placenta). Its expression is often complementary to the expression of VEGF (MIM 192240), suggesting that these molecules function in a coordinated manner. EG-VEGF potently contracts gastrointestinal (gi) smooth muscle. Induces proliferation, migration and fenestration (the formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. Has little or no effect on a variety of other endothelial and non-endothelial cell types.
Synonyms
PK1, Prokineticin 1, EG-VEGF, Prok1, Endocrine-gland-derived vascular endothelial growth factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized EG-VEGF Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EG-VEGF 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 Endocrine Gland Vascular Endothelial Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AVITGACERD IQCGAGTCCA ISLWLRGLRL CTPLGREGEE CHPGSHKIPF LRKRQHHTCP CSPSLLCSRF PDGRYRCFRD LKNANF.
Background
What is the molecular weight/Mw of EG-VEGF Protein?
EG-VEGF Protein has a total Mw of 9.6kDa.

What is the source or expression system of EG-VEGF Protein?
Escherichia Coli.

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

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

What is the amino acid sequence of EG-VEGF Protein?
AVITGACERD IQCGAGTCCA ISLWLRGLRL CTPLGREGEE CHPGSHKIPF LRKRQHHTCP CSPSLLCSRF PDGRYRCFRD LKNANF.

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

What is the endotoxin level for EG-VEGF Protein?
The endotoxin level is minimal, EG-VEGF 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:

Hairy and Enhancer of Split 7 Human Recombinant

Hairy and enhancer of split 7, bHLHb37, SCDO4, Transcription factor HES-7, HES7, hHes7, Class B basic helix-loop-helix protein 37, bHLH factor Hes7.

Product # :

PRO-1306

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

HES7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 253 amino acids (1-230) and having a molecular mass of 27kDa. HES7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The HES7 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

More Info

Introduction
HES7 belongs to the Hairy and enhancer of split family of bHLH transcription factors. The mouse ortholog of the HES7 is set by Notch signaling. The protein serves as a transcriptional repressor, and is involved in correct patterning of the axial skeleton. A mutation in HES7 has been shown to result in spondylocostal dysostosis. Multiple transcript variants encoding different isoforms have been discovered for HES7.
Synonyms
Hairy and enhancer of split 7, bHLHb37, SCDO4, Transcription factor HES-7, HES7, hHes7, Class B basic helix-loop-helix protein 37, bHLH factor Hes7.
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 MGSMVTRDRA ENRDGPKMLK PLVEKRRRDR INRSLEELRL LLLERTRDQN LRNPKLEKAE ILEFAVGYLR ERSRVEPPAA AAPGVPRSPV QDAEALASCY LSGFRECLLR LAAFAHDASP AARAQLFSAL HGYLRPKPPR PKPVDPRPPA PRPSLDPAAP ALGPALHQRP PVHQGHPSPR CAWSPSLCSP RAGDSGAPAP LTGLLPPPPP PHRQDGAPKA PLPPPPAFWR PWP.

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:

Epidermal Growth Factor, His Active Mouse Recombinant

AI790464, Pro-epidermal growth factor, URG.

Product # :

CYT-1054

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
biological activity
More Info
SDS-PAGE
Citations

Description

EGF Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids (977-1029 a.a) and having a molecular mass of 8.6kDa.EGF is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

EGF protein solution (0.25mg/ml) contains 10% glycerol, 20mM Tris-HCl (pH 8.0), 0.1M NaCl & 2mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Measured in a cell proliferation assay using mouse Balb/3T3 cell. The ED50 for this effect less or equal to 1ng/ml.

SDS-PAGE

More Info

Introduction
Pro-Epidermal Growth Factor Isoform 1 or EGF, is a globular peptide (77aa residues) which includes three intra molecular disulfide bonds. This protein acts as a growth factor that mediates the growth and proliferation of different epithelial & epidermal cells. Among other processes that EGF is part of are inhibition of gastric secretion and wound healing. EGF is a ligand for class I tyrosine kinase receptor (c-erbB).
Synonyms
AI790464, Pro-epidermal growth factor, URG.
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 MGSMNSYPGC PSSYDGYCLN GGVCMHIESL DSYTCNCVIG YSGDRCQTRD LRWWELR.
Background
Deciphering Epidermal Growth Factor Signaling: Unveiling the Potential of His-Tagged Active Mouse Recombinant
Abstract:
This research paper delves into the intricate realm of Epidermal Growth Factor (EGF) signaling, focusing on the novel application of Histidine (His)-tagged Active Mouse Recombinant EGF. By employing sophisticated methodologies encompassing protein engineering, receptor binding assays, and cellular response analyses, this study sheds light on the multifaceted molecular attributes and therapeutic prospects of this innovative variant.
Introduction:
Epidermal Growth Factor (EGF) orchestrates pivotal cellular processes. This paper delves into the intricate signaling dynamics of EGF, with a spotlight on the innovative approach of utilizing His-Tagged Active Mouse Recombinant EGF to unravel its complexities and therapeutic potential.
Protein Engineering and His-Tag Integration:
The study embarks on strategic protein engineering, introducing a Histidine (His) Tag to the Active Mouse Recombinant EGF. This His-Tag facilitates purification and subsequent analyses, enabling a comprehensive exploration of EGF signaling.
Receptor Binding Assays and Ligand Interaction:
Advanced receptor binding assays unravel the nuances of EGF's interaction with its cognate receptor, including affinities and kinetics. By employing His-Tagged EGF, the study dissects the impact of the tag on receptor binding, shedding light on its potential implications on downstream signaling.
Cellular Responses and Pathway Activation:
In vitro cellular assays unveil the complex web of signaling pathways triggered by EGF. The study employs high-throughput techniques to investigate the intricate cascades initiated by His-Tagged Active Mouse Recombinant EGF, providing insights into its potential role in cell proliferation, migration, and survival.
Structural Dynamics and Conformational Insights:
In-depth biophysical analyses, including nuclear magnetic resonance (NMR) spectroscopy, delve into the structural dynamics of His-Tagged EGF. This sheds light on potential conformational changes induced by the tag and their impact on receptor binding affinity.
Therapeutic Implications and Future Prospects:
The integration of a His Tag not only facilitates purification but also offers avenues for targeted therapies. His-Tagged EGF could serve as a platform for tailored drug delivery, enhancing the precision of interventions in various pathologies.
Challenges and Future Research Directions:
While the His Tag offers immense potential, challenges such as potential interference with receptor binding warrant scrutiny. Future research should focus on optimizing the positioning of the tag and exploring its impact on downstream signaling cascades.
Conclusion:
In a synthesis of innovative methodologies and visionary insights, the integration of a His Tag into Active Mouse Recombinant EGF emerges as a paradigm-shifting approach. This technique not only enriches our understanding of EGF signaling dynamics but also presents exciting prospects for personalized therapeutic interventions.
What is the molecular weight/Mw of EGF MOUSE, HIS ACTIVE Protein?
EGF MOUSE, HIS ACTIVE Protein has a total Mw of 8.6kDa.

What is the source or expression system of EGF MOUSE, HIS ACTIVE Protein?
Escherichia Coli.

What is the Purity of EGF MOUSE, HIS ACTIVE Protein?
EGF MOUSE, HIS ACTIVE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of EGF MOUSE, HIS ACTIVE Protein?
Measured in a cell proliferation assay using mouse Balb/3T3 cell. The ED50 for this effect less or equal to 1ng/ml.

What is the amino acid sequence of EGF MOUSE, HIS ACTIVE Protein?
MGSSHHHHHH SSGLVPRGSH MGSMNSYPGC PSSYDGYCLN GGVCMHIESL DSYTCNCVIG YSGDRCQTRD LRWWELR.
What applications can EGF MOUSE, HIS ACTIVE Protein be used in?
EGF MOUSE, HIS ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EGF MOUSE, HIS ACTIVE Protein?
The endotoxin level is minimal, EGF MOUSE, HIS ACTIVE 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:

Interleukin-1 beta Mouse Recombinant, His Tag

Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta, Interleukin-1 beta.

Product # :

CYT-578

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

Interleukin-1 beta Mouse Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 189 amino acids and having a molecular mass of 21 kDa. The IL-1b is fused to His-Tag and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The IL-1B protein contains 20mM Tris pH-8 and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Interleukin-1b is produced by activated macrophages, IL-1B stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1B proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells. IL-1b is an inflammatory cytokine which modulates angiogenesis by interacting directly with vascular endothelial cells & increasing the production of proangiogenic factors through paracrine control. IL-1 beta stimulates endothelial cell migration and proliferation, adhesion-molecule expression, inflammatory mediator production, and leukocyte recruitment. IL1B is essential for tumor growth, metastasis, and angiogenesis in quite a few animal models.
Synonyms
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta, Interleukin-1 beta.
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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMVPI RQLHYRLRDE QQKSLVLSDP YELKALHLNG QNINQQVIFS MSFVQGEPSN DKIPVALGLK GKNLYLSCVM KDGTPTLQLE SVDPKQYPKK KMEKRFVFNK IEVKSKVEFE SAEFPNWYIS TSQAEHKPVF LGNNSGQDII DFTMESVSS.
Background
What is the molecular weight/Mw of IL1B MOUSE, HIS Protein?
IL1B MOUSE, HIS Protein has a total Mw of 21kDa.

What is the source or expression system of IL1B MOUSE, HIS Protein?
Escherichia Coli.

What is the Purity of IL1B MOUSE, HIS Protein?
IL1B MOUSE, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1B MOUSE, HIS Protein?
The biological functionality of IL1B MOUSE, HIS Protein will be determined in the future.

What is the amino acid sequence of IL1B MOUSE, HIS Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMVPI RQLHYRLRDE QQKSLVLSDP YELKALHLNG QNINQQVIFS MSFVQGEPSN DKIPVALGLK GKNLYLSCVM KDGTPTLQLE SVDPKQYPKK KMEKRFVFNK IEVKSKVEFE SAEFPNWYIS TSQAEHKPVF LGNNSGQDII DFTMESVSS.

What applications can IL1B MOUSE, HIS Protein be used in?
IL1B MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1B MOUSE, HIS Protein?
The endotoxin level is minimal, IL1B MOUSE, HIS 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:

N-Ethylmaleimide-Sensitive Factor Attachment Protein, Alpha Human Recombinant

SNAPA, SNAP-alpha.

Product # :

PRO-250

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

NAPA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-295) and having a molecular mass of 35.3 kDa. NAPA is fused to 20 amino acid His Tag at N-terminus and purified by standard chromatography techniques.

Source

Escherichia Coli.

Formulation

NAPA protein solution (1mg/ml) contains 20mM Tris-HCl pH-7.5 and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
NAPA is part of the SNAP (Soluble NSF Attachment Protein) family. SNAPs, acting together with SNAREs (SNAP receptors) and the N-ethylmaleimide-sensitive fusion protein (NSF), are necessary for the fusion of transport vesicles to their objective membranes in synaptic transmission, intra-Golgi transport, endosome-to-endosome fusion and transcytotic vesicles-to-plasma membrane transport. NAPA is in charge of the binding of NSF and therefore the formation of a 20S fusion particle.
Synonyms
SNAPA, SNAP-alpha.
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 MDNSGKEAEA MALLAEAERK VKNSQSFFSG LFGGSSKIEE ACEIYARAAN MFKMAKNWSA AGNAFCQAAQ LHLQLQSKHD AATCFVDAGN AFKKADPQEA INCLMRAIEI YTDMGRFTIA AKHHISIAEI YETELVDIEK AIAHYEQSAD YYKGEESNSS ANKCLLKVAG YAALLEQYQK AIDIYEQVGT NAMDSPLLKY SAKDYFFKAA LCHFCIDMLN AKLAVQKYEE LFPAFSDSRE CKLMKKLLEA
HEEQNVDSYT ESVKEYDSIS RLDQWLTTML LRIKKTIQGD EEDLR.

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:

Leptin N82K Human Recombinant, Pegylated

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-1107

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

Pegylated Leptin N82K Human Recombinant produced in E.Coli is a single non-glycosilated polypeptide chain containing 146 amino acids, an additional Ala at N-terminus and one molecule of PEG 20 kDa at its N-terminus acids and having a molecular weight of 35.6kDa. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. Pegylated Leptin N82K Human Recombinant was purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3 Having 35-40% protein.

Purity

Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.

Biological Activity

Pegylated Leptin Human is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated Leptin in vitro activity is 5-7 fold lower than the non-pegylated recombinant human leptin but in vivo Pegylated Leptin has profound weight reducing effect (as compared to the non-pegylated recombinant human leptin), resulting mainly from reduced food intake.

More Info

Introduction
Leptin takes an important part in the regulation of energy balance and body weight control.After entering the circulation, Leptin binds LEPRwhich results in the activation of several major signalling pathways. In the hypothalamus Leptin acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption and also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, regulates pancreatic beta-cell function and insulin secretion and affects innate and adaptive immunity.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Pegylated Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Pegylated Leptin N82K 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 Pegylated Leptin in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 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:

Interleukin-11 Human Recombinant, Pichia

Interleukin-11, IL-11, Adipogenesis inhibitory factor, AGIF, Oprelvekin, IL11.

Product # :

CYT-013

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

IL11 Human Recombinant produced in Pichia Pastoris is a single, non-glycosylated, Polypeptide chain containing 177 amino acids (it differs from the 178 amino acid length of the native IL11 only in lack of the N-terminal praline residue) and having a molecular mass of 19kDa.The IL11 is purified by proprietary chromatographic techniques.

Source

Pichia Pastoris.

Formulation

IL11 was Lyophilized from a 0.2 µm filtered concentrated solution of 20mM PB, pH7.2 and 2% Glycine buffer.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

The ED50 as determined by the dose-dependent stimulation of the proliferation of murine 7TD1 was found to be less then 0.2ng-0.8ng/ml, corresponding to a Specific Activity of greater than 1,000,000 IU/ mg.

More Info

Introduction
IL11 is a member of the gp130 family of cytokines. These cytokines drive the assembly of multisubunit receptor complexes, all of which contain at least one molecule of the transmembrane signaling receptor IL6ST (gp130). IL-11 is shown to stimulate the T-cell-dependent development of immunoglobulin-producing B cells. It is also found to support the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells.
Synonyms
Interleukin-11, IL-11, Adipogenesis inhibitory factor, AGIF, Oprelvekin, IL11.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL11 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 Interleukin -11 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Pro-Pro-Pro-Gly.
Background
What is the molecular weight/Mw of IL11 HUMAN, PICHIA Protein?
IL11 HUMAN, PICHIA Protein has a total Mw of 19kDa.

What is the source or expression system of IL11 HUMAN, PICHIA Protein?
Pichia Pastoris.
What is the Purity of IL11 HUMAN, PICHIA Protein?
IL11 HUMAN, PICHIA Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL11 HUMAN, PICHIA Protein?
The ED50 as determined by the dose-dependent stimulation of the proliferation of murine 7TD1 was found to be less then 0.2ng-0.8ng/ml, corresponding to a Specific Activity of greater than 1,000,000 IU/ mg.

What is the amino acid sequence of IL11 HUMAN, PICHIA Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Pro-Pro-Pro-Gly.

What applications can IL11 HUMAN, PICHIA Protein be used in?
IL11 HUMAN, PICHIA Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL11 HUMAN, PICHIA Protein?
The endotoxin level is minimal, IL11 HUMAN, PICHIA Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL11 HUMAN, PICHIA that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL11 HUMAN, PICHIA?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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:

Pigment Epithelium-Derived Factor Human Recombinant

Pigment epithelium-derived factor,PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.

Product # :

CYT-580

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info
Citations

Description

PEDF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 400 amino acids and having a molecular mass of 44.5 kDa. The Human PEDF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The sterile filtered concentrated (1mg/ml) protein solution was lyophilized with 20mM sodium phosphate buffer & 150mM NaCl pH-7.4.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. PEDF is a 50,000 dalton glycoprotein created and secreted in many tissues all the way through the body. A key component of the anti-angiogenic action of PEDF is the induction of apoptosis in proliferating endothelial cells. Additionally, PEDF is capable to inhibit the activity of angiogenic factors such as VEGF and FGF-2. The neuro-protective effects of PEDF are achieved through suppression of neuronal apoptosis induced by peroxide, glutamate, or other neurotoxins. The recognition of a lipase-linked cell membrane receptor for PEDF (PEDF-R) that binds to PEDF with high affinity should facilitate further elucidation of the underlying mechanisms of this pluripotent serpin. To date, PEDF-R is the only signaling receptor known to be used by a serpin family member. The unique range of PEDF activities associate it as a potential therapeutic agent for the treatment of vasculature related neurodegenerative diseases such as age-related macular degeneration (AMD) and proliferative diabetic retinopathy (PDR). PEDF in addition has the potential to be functional in the treatment of various angiogenesis-related diseases including a number of cancers.
Synonyms
Pigment epithelium-derived factor,PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PEDF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PEDF Human 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 PEDF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MQNPASPPEE GSPDPDSTGA LVEEEDPFFK VPVNKLAAAV SNFGYDLYRV RSSMSPTTNV LLSPLSVATA LSALSLGAEQ RTESIIHRAL YYDLISSPDI HGTYKELLDT VTAPQKNLKS ASRIVFEKKL RIKSSFVAPL EKSYGTRPRV LTGNPRLDLQ EINNWVQAQM KGKLARSTKE IPDEISILLL GVAHFKGQWV TKFDSRKTSL EDFYLDEERT VRVPMMSDPK AVLRYGLDSD LSCKIAQLPL TGSMSIIFFL PLKVTQNLTL IEESLTSEFI HDIDRELKTV QAVLTVPKLK LSYEGEVTKS LQEMKLQSLF DSPDFSKITG KPIKLTQVEH RAGFEWNEDG AGTTPSPGLQ PAHLTFPLDY HLNQPFIFVL RDTDTGALLF IGKILDPRGP.
Background
About PEDF Human
Also known as “Pigment Epithelium-Derived Factor” or “SERPINF1,” PEDF is a
multifunctional protein found in vertebrates. It has anti-tumorigenic, anti-angiogenic, and
neurotrophic functions. Currently, it’s being researched as a candidate for treatment for
several conditions, including heart disease and cancer.
What’s the Function of PEDF Human Recombinant?
PEDF is created/secreted in several tissues across the body. It has a unique anti-angiogenic
action because of its induction of apoptosis in proliferating endothelial cells. Also, PEDF
can inhibit many angiogenic factors, including VEGF and FGF-2. PEDF-R is currently the
only known signaling receptor to be used by a serpin family member.

What’s the Application of PEDF Human Recombinant?
This version of PEDF is produced in E. Coli. It’s a single, non-glycosylated, polypeptide
chain that contains 400 amino acids. It has a molecular mass of 44.5 kDa, and it’s purified
by proprietary chromatographic techniques.
The main purpose of PEDF human recombinant is for research. It has the potential to
become a potential treatment for different angiogenesis-related diseases, including
various cancers. Moreover, it can become crucial during the recovery from vasculature-
related neurodegenerative illness.
Such a discovery could be revolutionary for the world, which is why more research is
needed to determine the effect of this non-inhibitory serpin on the body.

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:

Melanoregulin Human Recombinant

Melanoregulin, DSU, Dilute Suppressor Protein Homolog, WDT2, Whn-Dependent Transcript 2.

Product # :

PRO-1885

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

MREG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-214 a.a) and having a molecular mass of 27.3kDa.MREG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
Melanoregulin (MREG) takes part in membrane fusion and in regulating the biogenesis of disk membranes of photoreceptor rods. MREG is expressed in photoreceptor cells as two isoforms as a result of alternative splicing. MREG interacts with Peripherin-2, a photoreceptor specific tetraspanin protein which is required to preserve normal cell structure during the renewal process of membrane fusion. Moreover, MREG plays a part in the incorporation of pigments into hair.
Synonyms
Melanoregulin, DSU, Dilute Suppressor Protein Homolog, WDT2, Whn-Dependent Transcript 2.
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).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMGLRDWL RTVCCCCGCE CLEERALPEK EPLVSDNNPY SSFGATLVRD DEKNLWSMPH DVSHTEADDD RTLYNLIVIR NQQAKDSEEW QKLNYDIHTL RQVRREVRNR WKCILEDLGF QKEADSLLSV TKLSTISDSK NTRKAREMLL KLAEETNIFP TSWELSERYL FVVDRLIALD AAEEFFKLAR RTYPKKPGVP CLADGQKELH YLPFPSP

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:

GH Mouse Recombinant

GH1, GH, GHN, GH-N, hGH-N, Pituitary GH, GH-1.

Product # :

CYT-540

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info
Citations

Description

Growth Hormone Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 190 amino acids and having a molecular mass of 22 kDa. Mouse GH is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Mouse Growth Hormone Recombinant Lyophilized from a 0.2 μm filtered solution of 20mM HEPES, 4% Sucrose, 4% Mannitol, 0.02% Tween 80, pH 8.0.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
GH is a member of the prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the GH locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five GHs, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the GH locus. Mutations in or deletions of the gene lead to GH deficiency and short stature.
Synonyms
GH1, GH, GHN, GH-N, hGH-N, Pituitary GH, GH-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GH mouse although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GH mouse 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 Growth Hormone Murine in sterile 18MΩ-cm H2O not less than 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:

Midkine Rat Recombinant

Midkine, MK, Mdk.

Product # :

CYT-747

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

Midkine Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 120 amino acids and having a molecular mass of 13.2kDa.The Midkine Rat is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

Purity

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

Biological Activity

The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration range of 10-100 ng/ml.

More Info

Introduction
Midkine (MK) is the product of a retinoic acid responsive gene, MK, and is a member of a family of heparin binding factors. It contains 121 amino acid residues including 10 conserved cysteine residues, all of which appear to be disulphide linked.
Midkine is expressed during embryogenesis, showing an expression pattern that suggests functions in neurogenesis, cell migration, secondary organogenetic induction, and mesoderm-epithelial interaction.
The widespread downregulation of MK in the adult human is reverted in a number of cancers, in which polypeptides are able to act as both transforming growth factors and promoters of angiogenesis.
Midkine (MK), induces chemotaxis of human neutrophils and was found to trigger mobilization of intracellular calcium of these cells.
Midkine induces histamine release from rat peritoneal mast cells with a rapid response in a dose dependent manner.
Midkine is also a potent stimulator of collagen and glycosaminoglycan synthesis.
Synonyms
Midkine, MK, Mdk.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Midkine Rat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Midkine Rat 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 Midkine Rat in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VAKKKDKVKK GSECSEWTWG PCTPSSKDCG MGFREGTCGA QTQRIHCKVP CNWKKEFGAD CKYKFESWGA CDGSTGTKAR QGTLKKARYN AQCQETIRVT KPCTSKTKSK AKAKKGKGKD.

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:

Nuclear Factor Erythroid 2-Like 2 Human Recombinant

NFE2L2, Nuclear factor erythroid 2-related factor 2, NF-E2-related factor 2, NFE2-related factor 2, HEBP1, Nuclear factor, erythroid derived 2, like 2, NRF2.

Product # :

PRO-2167

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

NFE2L2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 625 amino acids (1-605 a.a) and having a molecular mass of 69.9kDa.NFE2L2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

NFE2L2 protein solution (0.25mg/ml) in Phosphate buffer saline (pH 7.4) containing 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

More Info

Introduction
Nuclear factor (erythroid-derived 2)-like 2 (NRF2) is bZIP transcription factors which heterodimerize with Maf proteins to bind Mare sequences. In addition, the NRF proteins bind the antioxidant response element (ARE) and are associated with the regulation of detoxification enzymes and the oxidative stress response. NRF2 is extensively expressed and is assumed to translocate to the nucleus after treatment with xenobiotics and antioxidants, which stimulate its release from its repressor protein, Keap1.
Synonyms
NFE2L2, Nuclear factor erythroid 2-related factor 2, NF-E2-related factor 2, NFE2-related factor 2, HEBP1, Nuclear factor, erythroid derived 2, like 2, NRF2.
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 MMDLELPPPG LPSQQDMDLI DILWRQDIDL GVSREVFDFS QRRKEYELEK QKKLEKERQE QLQKEQEKAF FAQLQLDEET GEFLPIQPAQ HIQSETSGSA NYSQVAHIPK SDALYFDDCM QLLAQTFPFV DDNEVSSATF QSLVPDIPGH IESPVFIATN QAQSPETSVA QVAPVDLDGM QQDIEQVWEE LLSIPELQCL NIENDKLVET TMVPSPEAKL TEVDNYHFYS SIPSMEKEVG NCSPHFLNAF EDSFSSILST EDPNQLTVNS LNSDATVNTD FGDEFYSAFI AEPSISNSMP SPATLSHSLS ELLNGPIDVS DLSLCKAFNQ NHPESTAEFN DSDSGISLNT SPSVASPEHS VESSSYGDTL LGLSDSEVEE LDSAPGSVKQ NGPKTPVHSS GDMVQPLSPS QGQSTHVHDA QCENTPEKEL PVSPGHRKTP FTKDKHSSRL EAHLTRDELR AKALHIPFPV EKIINLPVVD FNEMMSKEQF NEAQLALIRD IRRRGKNKVA AQNCRKRKLE NIVELEQDLD HLKDEKEKLL KEKGENDKSL HLLKKQLSTL YLEVFSMLRD EDGKPYSPSE YSLQQTRDGN VFLVPKSKKP DVKKN.

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:

Cysteine-Rich Angiogenic Inducer 61 Human Recombinant

CYR61, Protein CYR61, Cysteine-rich angiogenic inducer 61, IGF-binding protein 10, IGFBP-10, IBP-10, Protein GIG1, CCN family member 1, CCN1, GIG1, IGFBP10.

Product # :

CYT-164

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

CYR61 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 357 amino acids and having a molecular mass of 39.5kDa.The CYR61 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2m filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50 was determined by the proliferation of mouse 3T3 cells is < 2.0 ug/ml, corresponding to a specific activity of > 500 units/mg.

More Info

Introduction
CYR61 is a growth factor-inducible, immediate-early gene that has multifaceted activities in various cancers. CYR61 is a secreted, cysteine-rich, binding protein which is encoded by a growth factor-inducible immediate-early gene. Acting as an extracellular, matrix-associated signaling molecule, CYR61 promotes the adhesion of endothelial cells through interaction with integrin and enhances growth factor-induced DNA synthesis in the same cell type.
Synonyms
CYR61, Protein CYR61, Cysteine-rich angiogenic inducer 61, IGF-binding protein 10, IGFBP-10, IBP-10, Protein GIG1, CCN family member 1, CCN1, GIG1, IGFBP10.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CYR61 Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CYR61 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 CYR61 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TCPAACHCPL EAPKCAPGVG LVRDGCGCCK VCAKQLNEDC SKTQPCDHTK GLECNFGASS TALKGICRAQ SEGRPCEYNS RIYQNGESFQ PNCKHQCTCI DGAVGCIPLC PQELSLPNLG CPNPRLVKVT GQCCEEWVCD EDSIKDPMED QDGLLGKELG FDASEVELTR NNELIAVGKG SSLKRLPVFG MEPRILYNPL QGQKCIVQTT SWSQCSKTCG TGISTRVTND NPECRLVKET RICEVRPCGQ PVYSSLKKGK KCSKTKKSPE PVRFTYAGCL SVKKYRPKYC GSCVDGRCCT
PQLTRTVKMR FRCEDGETFS KNVMMIQSCK CNYNCPHANE AAFPFYRLFN DIHKFRD
Background
Title: Cysteine-Rich Angiogenic Inducer 61 Human Recombinant: A Potential Regulator of Angiogenesis
Abstract:

Cysteine-rich angiogenic inducer 61 (CYR61) is an important extracellular matrix-associated protein that plays a significant role in angiogenesis and cell adhesion. This research paper provides a comprehensive analysis of human recombinant CYR61, focusing on its production, characterization, and potential applications in regulating angiogenesis. The paper discusses the significance of CYR61 in physiological and pathological angiogenesis, including wound healing, tumor development, and cardiovascular diseases. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant CYR61 in various pathological conditions. The information presented in this paper aims to enhance our understanding of human recombinant CYR61 and its utility as a research tool and a potential regulator of angiogenesis.
Introduction:

Cysteine-rich angiogenic inducer 61 (CYR61) is an extracellular matrix-associated protein that plays a crucial role in angiogenesis, the formation of new blood vessels from pre-existing ones. Human recombinant CYR61, produced through genetic engineering techniques, provides researchers with a valuable tool to study its biological functions and explore its therapeutic potential.
Production and Characterization:

Recombinant CYR61 is typically generated using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Quality control measures are implemented to confirm the specificity and bioactivity of the recombinant CYR61.
Role in Angiogenesis:

CYR61 is involved in various aspects of angiogenesis, including endothelial cell proliferation, migration, and tube formation. It interacts with integrins and other cell surface receptors to modulate signaling pathways involved in angiogenic processes. Recombinant CYR61 serves as a valuable tool for studying the mechanisms underlying angiogenesis and exploring its potential as a therapeutic target.
Therapeutic Implications:

The dysregulation of angiogenesis is associated with several pathological conditions, including cancer, cardiovascular diseases, and chronic wounds. Recombinant CYR61 has shown promise as a potential regulator of angiogenesis and a therapeutic agent. It can be used to promote or inhibit angiogenesis, depending on the specific context. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant CYR61 in various diseases, including cancer and ischemic disorders.
Conclusion:

Human recombinant CYR61 is a valuable research tool and a potential regulator of angiogenesis. Its production, characterization, and applications in modulating angiogenic processes contribute to our understanding of angiogenesis and the development of novel therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant CYR61 offer promising prospects for improving outcomes in cancer, cardiovascular diseases, and wound healing.
What is the molecular weight/Mw of CCN1 Protein?
CCN1 Protein has a total Mw of 39.5kDa.

What is the source or expression system of CCN1 Protein?
Escherichia Coli.

What is the Purity of CCN1 Protein?
CCN1 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CCN1 Protein?
The ED50 was determined by the proliferation of mouse 3T3 cells is < 2.0 ug/ml, corresponding to a specific activity of > 500 units/mg.

What is the amino acid sequence of CCN1 Protein?
TCPAACHCPL EAPKCAPGVG LVRDGCGCCK VCAKQLNEDC SKTQPCDHTK GLECNFGASS TALKGICRAQ SEGRPCEYNS RIYQNGESFQ PNCKHQCTCI DGAVGCIPLC PQELSLPNLG CPNPRLVKVT GQCCEEWVCD EDSIKDPMED QDGLLGKELG FDASEVELTR NNELIAVGKG SSLKRLPVFG MEPRILYNPL QGQKCIVQTT SWSQCSKTCG TGISTRVTND NPECRLVKET RICEVRPCGQ PVYSSLKKGK KCSKTKKSPE PVRFTYAGCL SVKKYRPKYC GSCVDGRCCT
PQLTRTVKMR FRCEDGETFS KNVMMIQSCK CNYNCPHANE AAFPFYRLFN DIHKFRD

What applications can CCN1 Protein be used in?
CCN1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCN1 Protein?
The endotoxin level is minimal, CCN1 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:

Homeobox Protein NANOG, Mouse Anti Human

NANOG, Homeobox protein NANOG, Homeobox transcription factor Nanog, hNanog.

Product # :

ANT-422

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

formulation
More Info
Citations

Formulation

1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

More Info

Introduction
NANOG is a multidomain homeobox transcription factor which functions to maintain the undifferentiated state of pluripotent stem cells. NANOG expression counteracts the differentiation-promoting signals induced by the extrinsic factors LIF, Stat3 and BMP. Once NANOG expression is downregulated, cell differentiation can proceed. Proteins which regulate NANOG expression include transcription factors Oct4, SOX2, FoxD3, and Tcf3 and tumor suppressor p53.
Synonyms
NANOG, Homeobox protein NANOG, Homeobox transcription factor Nanog, hNanog.
Immunogen
Anti-human NANOG mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human NANOG amino acids 1-154 purified from E. coli.
Ig Subclass
Mouse IgG2a heavy chain and κ light chain.
Clone
P5A10AT.
Applications
NANOG antibody has been tested by ELISA, Western blot and immunohistochemistry analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot is 1:500~1:1,000 and immunohistochemistry analysis is 1:50~100. Recommended starting dilution for Western blot is 1:500 and Immunohistochemistry is 1:50.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
NANOG antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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:

Interleukin-3 Mouse Recombinant, sf9

Interleukin-3, Interleukin-3, sf9, IL3 sf9, L-3, Hematopoietic growth factor, Mast cell growth factor, MCGF, Multipotential colony-stimulating factor, P-cell-stimulating factor, Il3, Csfmu, Il-3, BPA, Csfmu, HCGF, Il-3, MCGF, PSF.

Product # :

CYT-922

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
biological activity
More Info
SDS-PAGE
Citations

Description

IL3 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 148 amino acids (27-166 a.a.) and having a molecular mass of 16.7kDa (Migrates at 18-28kDa on SDS-PAGE under reducing conditions).IL3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL3 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

The ED50 is Measured in a cell proliferation assay using TF-1 human erythroleukemic and is ≤ 0.1 ng/ml.

SDS-PAGE

More Info

Introduction
Interleukin-3 is a pleiotropic cytokine produced primarily by activated T cells.
IL-3 is thought to function via specific cell surface receptors to stimulate the proliferation, differentiation and survival of haematopoietic cell lines. IL-3 has also been shown to affect the functional activity of a variety of other cell types including mast cells, eosinophils, megakaryocytes and basophils.
Synonyms
Interleukin-3, Interleukin-3, sf9, IL3 sf9, L-3, Hematopoietic growth factor, Mast cell growth factor, MCGF, Multipotential colony-stimulating factor, P-cell-stimulating factor, Il3, Csfmu, Il-3, BPA, Csfmu, HCGF, Il-3, MCGF, PSF.
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
ASISGRDTHR LTRTLNCSSI VKEIIGKLPE PELKTDDEGP SLRNKSFRRV NLSKFVESQG EVDPEDRYVI KSNLQKLNCC LPTSANDSAL PGVFIRDLDD FRKKLRFYMV HLNDLETVLT SRPPQPASGS VSPNRGTVEC LEHHHHHH.
Background
What is the molecular weight/Mw of IL3 MOUSE, SF9 Protein?
IL3 MOUSE, SF9 Protein has a total Mw of 16.7kDa.

What is the source or expression system of IL3 MOUSE, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of IL3 MOUSE, SF9 Protein?
IL3 MOUSE, SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL3 MOUSE, SF9 Protein?
The ED50 is Measured in a cell proliferation assay using TF-1 human erythroleukemic and is ≤ 0.1 ng/ml.

What is the amino acid sequence of IL3 MOUSE, SF9 Protein?
ASISGRDTHR LTRTLNCSSI VKEIIGKLPE PELKTDDEGP SLRNKSFRRV NLSKFVESQG EVDPEDRYVI KSNLQKLNCC LPTSANDSAL PGVFIRDLDD FRKKLRFYMV HLNDLETVLT SRPPQPASGS VSPNRGTVEC LEHHHHHH.

What applications can IL3 MOUSE, SF9 Protein be used in?
IL3 MOUSE, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL3 MOUSE, SF9 Protein?
The endotoxin level is minimal, IL3 MOUSE, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL3 MOUSE, SF9 that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL3 MOUSE, SF9?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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:

4-1BB Receptor Human Recombinant

Tumor necrosis factor receptor superfamily member 9, 4-1BB ligand receptor T-cell, antigen 4-1BB homolog, T-cell antigen ILA, CD137 antigen, CDw137, ILA, 4-1BB, MGC2172, 4-1BBR, TNFRSF9.

Product # :

CYT-463

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

4-1BB Soluble Receptor Recombinant Human also called Tumor necrosis factor receptor superfamily member 9 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 167 amino acids, having a molecular mass of 17718 Dalton and containing the cysteine rich TNFR-like extracellular domain of 4-1BB Receptor. The 4-1BB Receptor is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.

Purity

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

Biological Activity

The activity was determined by the inhibition of 4-1BB ligand mediated stimulation of IL-8 production by human PBMC. Results: 90% inhibition using 1µg for both 4-1BB ligand and 4-1BB receptor.

More Info

Introduction
The protein encoded by this gene is a member of the TNF-receptor superfamily. This receptor contributes to the clonal expansion, survival, and development of T cells. It can also induce proliferation in peripheral monocytes, enhance T cell apoptosis induced by TCR/CD3 triggered activation, and regulate CD28 co-stimulation to promote Th1 cell responses. The expression of this receptor is induced by lymphocyte activation. TRAF adaptor proteins have been shown to bind to this receptor and transduce the signals leading to activation of NF-kappaB.
Synonyms
Tumor necrosis factor receptor superfamily member 9, 4-1BB ligand receptor T-cell, antigen 4-1BB homolog, T-cell antigen ILA, CD137 antigen, CDw137, ILA, 4-1BB, MGC2172, 4-1BBR, TNFRSF9.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized 4-1BB Receptor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution 4-1BBR 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 4-1BB Receptor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Glu-Arg-Thr-Arg.

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:

Recombinant Anti Human Epidermal Growth Factor Receptor

Product # :

ANT-600

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

Recombinant Anti Human Epidermal Growth Factor Receptor monoclonal antibody produced in CHO is a glycosylated dimer containing 1326 amino acids and having a molecular mass of 187.2 kDa.

Source

CHO.

Formulation

The protein 15.6mg/ml solution contains 20mmol/L Na2HPO4- NaH2PO4, 0.005% Tween 80, pH7.0.

Purity

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

Biological Activity

Compared with reference standard, the range of biological activity was found to be 86%.

More Info

Introduction
The epidermal growth factor receptor (EGF R) subfamily of receptor tyrosine kinases comprises four members: EGF R (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoprotein that has an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand-binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGF R gene encodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGF R has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-a , betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 in the absence of a co-receptor. Ligand binding induces EGF R homodimerization as well as heterdimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGF R can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGF R signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGF R signaling has also been shown to play a role in carcinogenesis.
Physical Appearance
Sterile filtered colorless liquid formulation.
Stability
Recombinant EGFR Antibody should be stored between 2-8°C. Please do not freeze.
Amino Acid Sequence
Heavy chain
QVQLKQSGPGLVQPSQSLSITCTVSGFSLTNYGVHWVRQSPGKGLEWLGVIWSGGNTDYNTP
FTSRLSINKDNSKSQVFFKMNSLQSNDTAIYYCARALTYYDYEFAYWGQGTLVTVSAASTKG
PSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSS
VVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPK
PKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTV
LHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVK
GFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEAL
HNHYTQKSLSLSPGK.
Light chain
DILLTQSPVILSVSPGERVSFSCRASQSIGTNIHWYQQRTNGSPRLLIKYASESISGIPSRF
SGSGSGTDFTLSINSVESEDIADYYCQQNNNWPTTFGAGTKLELKRTVAAPSVFIFPPSDEQ
LKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADY
EKHKVYACEVTHQGLSSPVTKSFNRGEC.

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:

SERTA Domain Containing 2 Human Recombinant

SERTA domain-containing protein 2, Transcriptional regulator interacting with the PHD-bromodomain 2, TRIP-Br2, SERTAD2, KIAA0127, SERTA domain containing 2, Sei-2.

Product # :

PRO-2021

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

SERTAD2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 337 amino acids (1-314) and having a molecular mass of 36.3 kDa.SERTAD2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The SERTAD2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
SERTA domain containing 2 (SERTAD2) takes part at E2F-responsive promoters to integrate signals which are given by PHD- and bromodomain-containing transcription factors. The SERTAD2 protein is taking part in modulating fat storage by down-regulating the expression of key genes which take part in thermogenesis, adipocyte lipolysis and oxidative metabolism.
Synonyms
SERTA domain-containing protein 2, Transcriptional regulator interacting with the PHD-bromodomain 2, TRIP-Br2, SERTAD2, KIAA0127, SERTA domain containing 2, Sei-2.
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 MGSMLGKGGK RKFDEHEDGL EGKIVSPCDG PSKVSYTLQR QTIFNISLMK LYNHRPLTEP SLQKTVLINN MLRRIQEELK QEGSLRPMFT PSSQPTTEPS DSYREAPPAF SHLASPSSHP CDLGSTTPLE ACLTPASLLE DDDDTFCTSQ AMQPTAPTKL SPPALLPEKD SFSSALDEIE ELCPTSTSTE AATAATDSVK GTSSEAGTQK LDGPQESRAD DSKLMDSLPG NFEITTSTGF LTDLTLDDIL FADIDTSMYD FDPCTSSSGT ASKMAPVSAD DLLKTLAPYS SQPVTPSQPF KMDLTELDHI MEVLVGS.

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:

Bone Morphogenetic protein-5 Human Recombinant

Bone morphogenetic protein 5, BMP-5, BMP5, MGC34244.

Product # :

CYT-660

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
sds-page
Citations

Description

BMP-5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 139 amino acids (317-454 a.a.) and having a total molecular mass of 15.7 kDa.BMP-5 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The BMP-5 solution contains 10mM Sodium Citrate buffer (pH3.5) and 10% Glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

sds-page

More Info

Introduction
BMP5 belongs to the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. This superfamily is comprised of large families of growth and differentiation factors. Bone morphogenetic proteins were initially identified by their ability of demineralizing bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site.
BMP5 is an essential signaling molecule within the trabecular meshwork and optic nerve head, and may play a potential role in glaucoma pathogenesis. It was shown that BMP-5 increases the levels of osteopontin, BMP-2, alkaline phosphatase and core binding factor alpha 1 mRNAs in human periodontal (HPL) ligament cells. The BMP5 protein is expressed in normal synovial tissue and reduced in osteoarthritis and rheumatoid arthritis. BMP5 may have a role in certain cancers given that it is differentially regulated during the formation of different tumors.
Synonyms
Bone morphogenetic protein 5, BMP-5, BMP5, MGC34244.
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
MAANKRKNQN RNKSSSHQDS SRMSSVGDYN TSEQKQACKK HELYVSFRDL GWQDWIIAPE GYAAFYCDGE CSFPLNAHMN ATNHAIVQTL VHLMFPDHVP KPCCAPTKLN AISVLYFDDS SNVILKKYRN MVVRSCGCH.
Background
Bone Morphogenetic Protein-5 Human Recombinant: Unleashing the Potential for Tissue Engineering and Regenerative Medicine
Abstract:
Bone Morphogenetic Protein-5 (BMP-5) human recombinant is a pivotal member of the bone morphogenetic protein family, known for its crucial role in tissue development, repair, and regeneration. This research paper provides an in-depth analysis of BMP-5, including its characteristics, signaling pathways, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMP-5 human recombinant are proposed, shedding light on its future implications in the field of tissue engineering and regenerative medicine.
Introduction:
Tissue engineering and regenerative medicine hold great promise for addressing the challenges of tissue repair and regeneration. BMP-5, a prominent member of the BMP family, plays a vital role in orchestrating cellular responses during tissue development and healing. This paper explores the unique features of BMP-5 and presents novel approaches for the production and optimization of BMP-5 human recombinant, aiming to unlock its therapeutic potential in various regenerative contexts.
Characteristics and Signaling Pathways:
BMP-5 is a secreted growth factor that belongs to the transforming growth factor-beta (TGF-β) superfamily. It exerts its biological effects by binding to specific cell surface receptors, initiating intracellular signaling cascades. BMP-5 signaling pathways, including Smad-dependent and Smad-independent pathways, regulate crucial processes such as cell differentiation, proliferation, and extracellular matrix synthesis, thereby influencing tissue development and repair.
Production of BMP-5 Human Recombinant:
Efficient production methodologies are crucial for harnessing the therapeutic potential of BMP-5 human recombinant. Recombinant protein expression systems, including mammalian cells or baculovirus-insect cell systems, have been utilized for the production of functional BMP-5. Optimization strategies, such as codon optimization, signal peptide engineering, and protein folding enhancement, have been employed to improve the yield and bioactivity of BMP-5 recombinant protein.
Potential Therapeutic Applications:
BMP-5 human recombinant holds tremendous potential in the field of tissue engineering and regenerative medicine. It plays a crucial role in bone formation, cartilage regeneration, and wound healing, making it a promising candidate for the treatment of skeletal disorders, osteochondral defects, and tissue injuries. Furthermore, the ability of BMP-5 to modulate cell behavior and tissue remodeling highlights its broader therapeutic applications in diverse regenerative processes.
Conclusion:
BMP-5 human recombinant emerges as a key regulator in tissue engineering and regenerative medicine, with significant implications for tissue repair and regeneration. Optimizing production methodologies and further elucidating its signaling mechanisms will enhance its therapeutic applications. With its involvement in bone and cartilage formation, as well as wound healing, BMP-5 human recombinant represents a promising tool for promoting tissue regeneration and addressing the challenges of tissue repair in various clinical contexts.
What is the molecular weight/Mw of BMP5 Protein?
BMP5 Protein has a total Mw of 15.7kDa.

What is the source or expression system of BMP5 Protein?
Escherichia Coli.

What is the Purity of BMP5 Protein?
BMP5 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BMP5 Protein?
The biological functionality of BMP5 Protein will be determined in the future.

What is the amino acid sequence of BMP5 Protein?
MAANKRKNQN RNKSSSHQDS SRMSSVGDYN TSEQKQACKK HELYVSFRDL GWQDWIIAPE GYAAFYCDGE CSFPLNAHMN ATNHAIVQTL VHLMFPDHVP KPCCAPTKLN AISVLYFDDS SNVILKKYRN MVVRSCGCH.

What applications can BMP5 Protein be used in?
BMP5 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BMP5 Protein?
The endotoxin level is minimal, BMP5 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:

Epidermal Growth Factor Rat Recombinant

Urogastrone, URG, EGF.

Product # :

CYT-669

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

Epidermal Growth Factor Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6151 Dalton. The Rat EGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Rat EGF was lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in PBS, pH 7.4.

Purity

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

Biological Activity

The ED50 as calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells is less than 0.1ng/ml, corresponding to a specific activity of > 10,000,000 units/mg.

More Info

Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide.
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Rat EGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Rat EGF 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 Rat EGF in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
NSNTGCPPSY DGYCLNGGVC MYVESVDRYV CNCVIGYIGE RCQHRDLRWW KLR.
Background
Pioneering Insights into Epidermal Growth Factor Rat Recombinant: Unraveling Signaling Dynamics and Therapeutic Implications
Abstract:
This research paper delves into the unexplored landscape of Epidermal Growth Factor Rat Recombinant (EGF-RR), delving into its intricate molecular attributes, signaling pathways, and potential therapeutic applications. By employing advanced methodologies encompassing protein expression, receptor binding assays, and bioinformatics analyses, this study sheds light on the complex interplay between EGF-RR and cellular responses, offering a new perspective for therapeutic interventions.
Introduction:
Epidermal Growth Factor (EGF) holds a key role in cellular regulation. This paper navigates the intricacies of Epidermal Growth Factor Rat Recombinant (EGF-RR), focusing on its unique molecular properties and its potential therapeutic implications.
Protein Expression and Purification:
The paper delves into the meticulous engineering of EGF-RR, involving gene optimization for enhanced expression. Protein purification strategies, such as affinity chromatography, are employed to obtain highly purified EGF-RR for subsequent analyses.
Receptor Binding Assays and Ligand Interaction:
Advanced receptor binding assays elucidate the interaction of EGF-RR with its cognate receptor. By quantifying binding affinities and kinetic rates, the study unveils the nuances of EGF-RR's engagement with its receptor, shedding light on potential structural determinants.
Cellular Signaling Pathways and Functional Responses:
Through in vitro cellular assays, the study unravels the intricate signaling pathways initiated by EGF-RR. Quantitative phosphoproteomic analyses expose the dynamic phosphorylation events triggered by EGF-RR, providing insights into its role in cellular proliferation, migration, and differentiation.
Bioinformatics Insights and Molecular Modeling:
Utilizing advanced bioinformatics tools, molecular dynamics simulations provide a deeper understanding of EGF-RR's interactions with its receptor and potential downstream effectors. Structural modeling unveils the conformational changes driving signaling cascades.
Therapeutic Prospects and Novel Avenues:
The molecular insights into EGF-RR's signaling dynamics open avenues for therapeutic exploration. Targeted interventions harnessing EGF-RR's potential in wound healing and tissue regeneration, as well as its role in modulating cancer microenvironments, emerge as promising prospects.
Challenges and Future Directions:
Despite progress, challenges such as deciphering context-dependent signaling responses remain. Future research should focus on unraveling the intricate cross-talk between different signaling pathways and exploring EGF-RR's role in specific disease contexts.
Conclusion:
In a convergence of advanced methodologies and visionary insights, Epidermal Growth Factor Rat Recombinant emerges as a captivating subject. Its distinctive molecular attributes and complex cellular interplay offer potential avenues for therapeutic interventions, ushering in a new era of precision medicine.
What is the molecular weight/Mw of EGF RAT Protein?
EGF RAT Protein has a total Mw of 6.1kDa.

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

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

What is the Biological Activity of EGF RAT Protein?
The ED50 as calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells is less than 0.1ng/ml, corresponding to a specific activity of > 10,000,000 units/mg.

What is the amino acid sequence of EGF RAT Protein?
NSNTGCPPSY DGYCLNGGVC MYVESVDRYV CNCVIGYIGE RCQHRDLRWW KLR.

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

What is the endotoxin level for EGF RAT Protein?
The endotoxin level is minimal, EGF RAT 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.

Country/region

Search results

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Formulation

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

SDS-PAGE

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info