Search: 1000 results found for "Growth Hormone"

Description:

Fibroblast Growth Factor-19 Human Recombinant, HEK

fibroblast growth factor 19, FGF19.

Product # :

CYT-1180

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Description

FGF19 Mouse Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 23-216) containing 205 amino acids and having a molecular mass of 23.0 kDa.FGF19 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

FGF19 protein (0.5mg/ml) contains 20mM Tris-HCl(pH8.0), 20% glycerol and 0.1M NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Fibroblast Growth Factor-19 (FGF-19) is a member of the FGF family. FGF-19 interacts with FGFR1, FGFR2, FGFR3 and FGFR4. T FGF-19 takes part in the suppression of bile acid biosynthesis through downregulation of CYP7A1 expression, following positive regulation of the JNK and EPK1/2 cascades. FGF-19 stimulates glucose uptake in adiposytes and is a high affinity, heparin dependent ligand for FGFR4.
Synonyms
fibroblast growth factor 19, FGF19.
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
DGSHMRPLAF SDAGPHVHYG WGDPIRLRHL YTSGPHGLSS CFLRIRADGV VDCARGQSAH SLLEIKAVAL RTVAIKGVHS VRYLCMGADG KMQGLLQYSE EDCAFEEEIR PDGYNVYRSE KHRLPVSLSS AKQRQLYKNR GFLPLSHFLP MLPMVPEEPE DLRGHLESDM FSSPLETDSM DPFGLVTGLE AVRSPSFEKH HHHHH
Background
What is the molecular weight/Mw of FGF19 HUMAN,HEK Protein?
FGF19 HUMAN,HEK Protein has a total Mw of 23kDa.

What is the source or expression system of FGF19 HUMAN,HEK Protein?
HEK293 cells.

What is the Purity of FGF19 HUMAN,HEK Protein?
FGF19 HUMAN,HEK Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF19 HUMAN,HEK Protein?
The biological functionality of FGF19 HUMAN,HEK Protein will be determined in the future.

What is the amino acid sequence of FGF19 HUMAN,HEK Protein?
DGSHMRPLAF SDAGPHVHYG WGDPIRLRHL YTSGPHGLSS CFLRIRADGV VDCARGQSAH SLLEIKAVAL RTVAIKGVHS VRYLCMGADG KMQGLLQYSE EDCAFEEEIR PDGYNVYRSE KHRLPVSLSS AKQRQLYKNR GFLPLSHFLP MLPMVPEEPE DLRGHLESDM FSSPLETDSM DPFGLVTGLE AVRSPSFEKH HHHHH

What applications can FGF19 HUMAN,HEK Protein be used in?
FGF19 HUMAN,HEK Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF19 HUMAN,HEK Protein?
The endotoxin level is minimal, FGF19 HUMAN,HEK 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:

GTP Cyclohydrolase I Feedback Regulator Human Recombinant

GFRP, HsT16933, P35,GTP cyclohydrolase 1 feedback regulatory protein, GTP cyclohydrolase I feedback regulatory protein, p35, GCHFR

Product # :

PRO-2006

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Description

GCHFR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 107 amino acids (1-84a.a) and having a molecular mass of 12.1kDa. GCHFR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GCHFR protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 40% glycerol and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
GTP Cyclohydrolase I Feedback Regulator, also known as GCHFR, is a Protein coding gene which includes a homodimer. GCHFR binds and mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase I. GCHFR also regulates phenylalanine metabolism in the liver and in the production of biogenic amine neurotransmitters and nitric oxide.
Synonyms
GFRP, HsT16933, P35,GTP cyclohydrolase 1 feedback regulatory protein, GTP cyclohydrolase I feedback regulatory protein, p35, GCHFR
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 MGSMPYLLIS TQIRMEVGPT MVGDEQSDPE LMQHLGASKR RALGNNFYEY YVDDPPRIVL DKLERRGFRV LSMTGVGQTL VWCLHKE.

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:

Connective Tissue Growth Factor Human Recombinant

CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.

Product # :

CYT-541

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Description

CTGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 98 amino acids and having a molecular mass of 11.2 kDa. The CTGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CTGF was Lyophilized from a sterile filtered aqueous solution containing 0.1% Trifluoroacetic Acid (TFA).

Purity

Purity of CTGF is greater than 90% as determined by SDS-PAGE.

Biological Activity

Determined by the dose-dependent stimulation of the proliferation of HUVEC cells. The expected ED50 for this effect is 1-2µg/ml, corresponding to a specific activity of 500-1000units/mg.

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Introduction
Connective Tissue Growth Factor belongs to the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 (Cystein rich 61), CTGF (Connective Tissue Growth Factor), Nov (Nephroblastoma Overexpressed gene), WISP-1, 2 and 3 (Wnt-1 Induced Secreted Proteins). The CCN genes encode secreted proteins associated with the Extracellular Matrix (ECM) and cell membrane.
CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: fibrosis, vascular ailments and tumorigenesis.
Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes.
The full length protein consists of four modulesModule I shares partial identity with the N-terminal part of the IGFBPs.
Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat (VWC).
Module III contains sequences sharing identity with the Thrombospondin type 1 repeat (TSP1) (WSXCSXXCG), which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion.
Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand's factor and mucins. Sequence similarities to binding motifs are also found within this domain.
Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy.
In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells.
CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.
Synonyms
CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CTGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTGF 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 CTGF in sterile 18MΩcm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MGKKCIRTPK ISKPIKFELS GCTSMKTYRA KFCGVCTDGR CCTPHRTTTL PVEFKCPDGE VMKKNMMFIK TCACHYNCPG DNDIFESLYY RKMYGDMA.
Background
Title: Connective Tissue Growth Factor Human Recombinant: Insights into Production, Function, and Therapeutic Potential
Abstract:

Connective tissue growth factor (CTGF) is a multifunctional protein that plays a critical role in tissue homeostasis and repair. This research paper provides a comprehensive analysis of human recombinant CTGF, focusing on its production, characterization, and potential therapeutic applications. The paper discusses the significance of CTGF in connective tissue development, fibrosis, and wound healing. Furthermore, it explores the ongoing research and clinical trials investigating the therapeutic potential of recombinant CTGF in various pathological conditions. The information presented in this paper aims to deepen our understanding of human recombinant CTGF and its utility as a research tool and a potential therapeutic agent.
Introduction:

Connective tissue growth factor (CTGF) is a secreted protein that belongs to the CCN (Cyr61, CTGF, Nov) family. It is involved in diverse cellular processes, including cell proliferation, extracellular matrix synthesis, and angiogenesis. Human recombinant CTGF, produced through genetic engineering techniques, enables researchers to study its biological functions and explore its therapeutic potential.
Production and Characterization:

Recombinant CTGF 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 biological activity of the recombinant CTGF.
Role in Tissue Homeostasis and Repair:

CTGF plays a critical role in connective tissue development, maintenance, and repair. It promotes the synthesis of extracellular matrix components, such as collagen and fibronectin, and regulates the activity of various growth factors. CTGF is also involved in wound healing and tissue remodeling processes. Understanding the molecular mechanisms underlying CTGF-mediated tissue repair provides insights into potential therapeutic interventions.
Therapeutic Implications:

The dysregulation of CTGF expression and signaling has been implicated in several pathological conditions, including fibrosis, arthritis, and cancer. Recombinant CTGF holds promise as a potential therapeutic agent for these diseases. Preclinical and clinical studies are being conducted to evaluate the safety and efficacy of CTGF-based therapies, such as CTGF-targeting antibodies and small-molecule inhibitors.
Conclusion:

Human recombinant CTGF is a valuable research tool and a potential therapeutic target in various pathological conditions. Its production, characterization, and applications in connective tissue biology contribute to our understanding of tissue repair mechanisms and the development of novel therapeutic strategies. Continued research and clinical trials exploring the therapeutic potential of recombinant CTGF offer promising avenues for improving patient outcomes.
What is the molecular weight/Mw of CTGF Protein?
CTGF Protein has a total Mw of 11.2kDa.

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

What is the Purity of CTGF Protein?
CTGF Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CTGF Protein?
Determined by the dose-dependent stimulation of the proliferation of HUVEC cells. The expected ED50 for this effect is 1-2µg/ml, corresponding to a specific activity of 500-1000units/mg.

What is the amino acid sequence of CTGF Protein?
MGKKCIRTPK ISKPIKFELS GCTSMKTYRA KFCGVCTDGR CCTPHRTTTL PVEFKCPDGE VMKKNMMFIK TCACHYNCPG DNDIFESLYY RKMYGDMA.

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

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

Placental Growth Factor-2, HEK Human Recombinant

PIGF, PGF, PlGF-2, PLGF-2.

Product # :

CYT-1228

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Description

PLGF2 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 19-170) containing 158 amino acids and having a molecular mass of 18.1kDa. PLGF2 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

PLGF2 protein (0.5mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured by its binding ability in a functional ELISA with Human VEGFR1/Flt-1.

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Synonyms
PIGF, PGF, PlGF-2, PLGF-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
LPAVPPQQWA LSAGNGSSEV EVVPFQEVWG RSYCRALERL VDVVSEYPSE VEHMFSPSCV SLLRCTGCCG DENLHCVPVE TANVTMQLLK IRSGDRPSYV ELTFSQHVRC ECRPLREKMK PERRRPKGRG KRRREKQRPT DCHLCGDAVP RRHHHHHH.
Background
PLGF2, a homodimeric glycoprotein, exhibits a unique structural configuration essential for its interactions with VEGF receptors and other signaling molecules. The human recombinant form provides a controlled platform for studying the three-dimensional structure of PLGF2, elucidating its binding affinities and conformational dynamics. Understanding its structure is fundamental for deciphering how PLGF2 mediates angiogenic signaling and vascular remodeling.

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:

Transforming Growth Factor-Beta 1 Human Recombinant

Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, LAP, TGFB1.

Product # :

CYT-716

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Description

TGFB1 Human Recombinant produced in CHO cells is a glycosylated homodimeric polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.6kDa. The TGFB1 is purified by proprietary chromatographic techniques.

Source

CHO cells.

Formulation

Lyophilized from a sterile filtered solution containing 0.1 % trifluoroacetic acid (TFA) And trehalose (1:20 protein to Trehalose ratio).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependent inhibition of IL-4-induced proliferation of HT-2 cells is 0.142ng/ml, corresponding to a specific activity of 7.4x10⁶units/mg.

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Introduction
Transforming growth factor betas (TGFBetas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
Synonyms
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, LAP, TGFB1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGFB1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB1 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 TGFB1 in sterile 10mM HCl at a concentration of 0.1 mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ALDTNYCFSS TEKNCCVRQL YIDFRKDLGW KWIHEPKGYH ANFCLGPCPY IWSLDTQYSK VLALYNQHNP GASAAPCCVP QALEPLPIVY YVGRKPKVEQ LSNMIVRSCK CS.
Background
Title: Transforming Growth Factor-Beta 1 Human Recombinant: A Promising Tool for Biomedical Research
Abstract:

Transforming Growth Factor-Beta 1 (TGF-β1) is a crucial cytokine involved in diverse cellular processes. This research paper provides an in-depth analysis of human recombinant TGF-β1, focusing on its production, purification, and applications in biomedical research. The paper discusses the significance of TGF-β1 in tissue engineering, regenerative medicine, and immunology. Furthermore, it elucidates the potential therapeutic implications of recombinant TGF-β1 in various diseases and highlights ongoing research in the field. The information presented in this paper aims to enhance the understanding of TGF-β1 and its utility as a research tool in biomedical sciences.
Introduction:

Transforming Growth Factor-Beta 1 (TGF-β1) is a multifunctional cytokine that regulates cellular processes such as cell growth, differentiation, and immune modulation. Human recombinant TGF-β1 is synthesized using genetic engineering techniques, enabling the production of large quantities of biologically active protein for research purposes.
Production and Purification:

Recombinant TGF-β1 is typically produced in expression systems such as bacteria, yeast, or mammalian cells. The protein is then purified using various chromatographic techniques to obtain a highly pure and active form. Quality control measures ensure the biological activity and integrity of the recombinant protein.
Biomedical Applications:

Human recombinant TGF-β1 has found broad applications in biomedical research. In tissue engineering and regenerative medicine, it plays a critical role in promoting cell proliferation, extracellular matrix production, and tissue repair. TGF-β1 is also involved in immune modulation, influencing immune cell differentiation and function. Recombinant TGF-β1 is a valuable tool for studying these processes and developing therapeutic interventions.
Therapeutic Implications:

The dysregulation of TGF-β1 signaling is associated with various diseases, including fibrosis, cancer, and autoimmune disorders. Recombinant TGF-β1 offers potential therapeutic applications through its ability to modulate cellular responses. Ongoing research aims to develop targeted therapies that specifically regulate TGF-β1 signaling for the treatment of these conditions.
Conclusion:

Human recombinant TGF-β1 holds immense potential as a research tool in biomedical sciences. Its production, purification, and applications in tissue engineering, regenerative medicine, and immunology contribute to advancing our understanding of cellular processes and disease mechanisms. With ongoing research, recombinant TGF-β1 may pave the way for novel therapeutic strategies in various medical fields.

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:

Insulin Like Growth Factor-1 N15 Labeled Human Recombinant

Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.

Product # :

CYT-128

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Description

IGF1 N15 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of 7.74kDa. The N15 is stable isotope labeled. The IGF1 N15 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IGF1 N15 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.

Purity

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

Biological Activity

The ED₅₀ as determined by a cell proliferation assay using serum free human MCF-7 cells is less than 2ng/ml, corresponding to a specific activity of > 5.0 × 10⁵ IU/mg.

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Introduction
The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).
Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IGF1 N15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 N15 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 IGF1 N15 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.

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:

Insulin Like Growth Factor-2 Mouse Recombinant

Somatomedin-A, IGF2, INSIGF, pp9974, C11orf43, FLJ22066, FLJ44734

Product # :

CYT-1196

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Description

IGF2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, monomeric polypeptide chain containing 67 amino acids and having a total molecular mass of 7.4kDa.The IGF2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a sterile (0.2µ) filtered solution containing 0.1 % trifluoroacetic acid (TFA).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by FDC-P1 cell proliferation is ≤ 50 ng/mL, corresponding to a specific activity of ≥ 2.0 x 10^4 units/mg.

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Introduction
Insulin-like growth factor II (IGF-II) is an important foetal growth hormone.IGF-II is made by theca cells during gestation. IGF-II binds the sink IGF-II receptor (IGF2R) which results in IGF-II degradation.IGF-II also engages the IGF-I receptor (IGF1R) to arbitrate embryonic growth.
Synonyms
Somatomedin-A, IGF2, INSIGF, pp9974, C11orf43, FLJ22066, FLJ44734
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF2 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 IGF2 in sterile water at a concentration of 0.1 mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AYGPGETLCG GELVDTLQFV CSDRGFYFSR PSSRANRRSR GIVEECCFRS CDLALLETYC ATPAKSE

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:

Placental Growth Factor Human Recombinant, His Tag

PIGF, PGF, PLGF-1.

Product # :

CYT-1031

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Description

PLGF1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 19-131) containing 123 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 13.8kDa (calculated).

Source

Escherichia Coli.

Formulation

PLGF1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in PBS and 5% w/v trehalose, pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
PLGF is a growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration. It binds to receptor vegfr-1/flt1.
Synonyms
PIGF, PGF, PLGF-1.
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 deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. PLGF1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHAS LPAVPPQQWA LSAGNGSSEV EVVPFQEVWG RSYCRALERL VDVVSEYPSE VEHMFSPSCV SLLRCTGCCG DENLHCVPVE TANVTMQLLK IRSGDRPSYV ELTFSQHVRC ECR.

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:

Thyroid Hormone Receptor Interactor 10 Human Recombinant

Cdc42-interacting protein 4, Protein Felic, Salt tolerant protein, hSTP, Thyroid receptor-interacting protein 10, TR-interacting protein 10, TRIP-10,TRIP10, CIP4, STOT, STP, HSTP.

Product # :

PRO-1811

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Description

TRIP10 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 309 amino acids (260-545) and having a molecular mass of 34.6 kDa.TRIP10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TRIP10 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol, 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Thyroid Hormone Receptor Interactor 10 (TRIP10) is a part of the F-BAR family of proteins which is expressed in a variety of tissues, including kidney, brain, liver, lung, heart and pancreas. The F-BAR family of proteins contains an N-terminal, alpha-helical, region which is hydrophobic and related to the Bin Amphiphysin Rvs (BAR) protein family. TRIP10 is vital for the coordination of membrane tubulation with Actin cytoskeletal reorganization during endocytosis.
Synonyms
Cdc42-interacting protein 4, Protein Felic, Salt tolerant protein, hSTP, Thyroid receptor-interacting protein 10, TR-interacting protein 10, TRIP-10,TRIP10, CIP4, STOT, STP, HSTP.
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 MGSDPKNDSH VLIELHKSGF ARPGDVEFED FSQPMNRAPS DSSLGTPSDG RPELRGPGRS RTKRWPFGKK NKTVVTEDFS HLPPEQQRKR LQQQLEERSR ELQKEVDQRE ALKKMKDVYE KTPQMGDPAS LEPQIAETLS NIERLKLEVQ KYEAWLAEAE SRVLSNRGDS LSRHARPPDP PASAPPDSSS NSASQDTKES SEEPPSEESQ DTPIYTEFDE DFEEEPTSPI GHCVAIYHFE GSSEGTISMA EGEDLSLMEE DKGDGWTRVR RKEGGEGYVP TSYLRVTLN.

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:

Progranulin Human Recombinant

GRN, PGRN, granulin, Acrogranin, propithelin, PC cell derived growth Factor, GEP, GP88, PEPI, PCDGF.

Product # :

CYT-524

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Quantity :

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Description

Progranulin Human Recombinant produced in HEK is a single, glycosylated, polypeptide chain containing 1-593 amino acids and having a molecular mass of 74kDa. The Progranulin is purified by standard chromatographic techniques.

Source

HEK 293 cells.

Formulation

The protein contains 1xPBS.

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

Activates phospho-ERK1/2 in neuronal mouse P19 cells and regulates food intake and body weight.

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Introduction
A 88-kDa progranulin, also called proepithelin and PC cell-derived growth factor, is a single precursor protein of granulins which are a family of secreted, glycosylated peptides that are cleaved from a single precursor protein with 7.5 repeats of a highly conserved 12-cysteine granulin/epithelin motif. Granulins are a variety of active, 6 kDa peptides and named granulin A (epithelin 1), granulin B (epithelin 2), granulin C, etc. Both the peptides and intact progranulin protein regulate cell growth. However, different members of the granulin protein family may act as inhibitors, stimulators, or have dual actions on cell growth. Granulin family members are important in normal development, wound healing, and tumorigenesis.
Synonyms
GRN, PGRN, granulin, Acrogranin, propithelin, PC cell derived growth Factor, GEP, GP88, PEPI, PCDGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Progranulin although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution PGRN should be stored at 4C between 2-7 days and for future use below -18C. 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 Progranulin 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:

Fibroblast Growth Factor 17 Mouse Recombinant

Fibroblast growth factor 17, FGF-17, FGF17, FGF-13, HH20.

Product # :

CYT-1123

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Description

Fibroblast Growth Factor 17 Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 194 amino acid and having a molecular mass of approximately 22.5kDa.FGF17 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in 20 mM Tris-HCl, pH 8.0, 0.02 % Tween-20 and 700 mM NaCl.

Purity

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

Biological Activity

The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is < 10 ng/ml, corresponding to a specific activity of > 1.0 × 105 IU/mg in the presence of 10 μg/ml of heparin.

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Introduction
Fibroblast Growth Factor 17 (FGF17) is a part of the fibroblast growth factor family. FGF family members have broad mitogenic and cell survival activities, and are involved in various biological processes includingmorphogenesis, embryonic development cell growth, , tissue repair, tumor growth and invasion. The FGF17 gene is highly expressed in the cerebellum and cortex. The mouse homolog of the FGF17 gene is localized to specific sites in the midline structures of the forebrain, the midbrain-hindbrain junction, developing skeleton and developing arteries, suggesting a part in central nervous system, bone and vascular development.
Synonyms
Fibroblast growth factor 17, FGF-17, FGF17, FGF-13, HH20.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor 17 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 17 in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TQGENHPSPN FNQYVRDQGA MTDQLSRRQI REYQLYSRTS GKHVQVTGRR ISATAEDGNK FAKLIVETDT FGSRVRIKGA ESEKYICMNK RGKLIGKPSG KSKDCVFTEI VLENNYTAFQ NARHEGWFMA FTRQGRPRQA SRSRQNQREA HFIKRLYQGQ LPFPNHAERQ KQFEFVGSAP TRRTKRTRRP QSQT.
Background
What is the molecular weight/Mw of FGF17 MOUSE Protein?
FGF17 MOUSE Protein has a total Mw of 22.5kDa.

What is the source or expression system of FGF17 MOUSE Protein?
Escherichia Coli.

What is the Purity of FGF17 MOUSE Protein?
FGF17 MOUSE Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF17 MOUSE Protein?
The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is < 10 ng/ml, corresponding to a specific activity of > 1.0 × 105 IU/mg in the presence of 10 μg/ml of heparin.

What is the amino acid sequence of FGF17 MOUSE Protein?
TQGENHPSPN FNQYVRDQGA MTDQLSRRQI REYQLYSRTS GKHVQVTGRR ISATAEDGNK FAKLIVETDT FGSRVRIKGA ESEKYICMNK RGKLIGKPSG KSKDCVFTEI VLENNYTAFQ NARHEGWFMA FTRQGRPRQA SRSRQNQREA HFIKRLYQGQ LPFPNHAERQ KQFEFVGSAP TRRTKRTRRP QSQT.

What applications can FGF17 MOUSE Protein be used in?
FGF17 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF17 MOUSE Protein?
The endotoxin level is minimal, FGF17 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:

Procalcitonin Canine Recombinant

Calcitonin, Calca, Calc, CCALCI.

Product # :

HOR-015

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Quantity :

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Description

Procalcitonin Canine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Ala26-Arg130) containing 115 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 12.7kDa.

Source

Escherichia Coli.

Formulation

Procalcitonin was filtered (0.4 µm) and lyophilized in 20mM TRIS and 50mM NaCl, pH 7.2.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.
Synonyms
Calcitonin, Calca, Calc, CCALCI.
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 deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Procalcitonin is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHASAPFRSALEGL PDPTALSEKE GRLLLAALVK AYVQRKNELE QEQEQETEGS SLDSSRAKRC SNLSTCVLGT YSKDLNNFHT FSGIGFGAET PGKKRDIASG LERGR.

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-6 Human Recombinant

Fibroblast Growth Factor 6, Heparin Secretory-Transforming Protein 2, Heparin-Binding Growth Factor 6, HBGF-6, HSTF-2, FGF-6, HST-2, HST2, HSTF2, FGF6.

Product # :

CYT-979

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Quantity :

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Description

FGF6 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain having containing 169 amino acids and having a molecular mass of 18.9kDa.The FGF-6 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FGF-6 protein was lyophilized from a 0.2µm filtered solution in 10mM sodium phosphate and 50mM sodium chloride pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Fibroblast Growth Factor-6 (FGF6) belongs to the fibroblast growth factor (FGF) family. FGF family members possess extensive mitogenic and cell survival functions, and are involved in various biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. The FGF6 gene displayes oncogenic transforming activity when transfected into mammalian cells. The mouse homolog of the FGF6 gene displays a restricted expression profile predominantly in the myogenic lineage, suggesting a role in muscle regeneration or differentiation.
Synonyms
Fibroblast Growth Factor 6, Heparin Secretory-Transforming Protein 2, Heparin-Binding Growth Factor 6, HBGF-6, HSTF-2, FGF-6, HST-2, HST2, HSTF2, FGF6.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-6 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 FGF6 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MGTRANNTLL DSRGWGTLLS RSRAGLAGEI AGVNWESGYL VGIKRQRRLY CNVGIGFHLQ VLPDGRISGT HEENPYSLLE ISTVERGVVS LFGVRSALFV AMNSKGRLYA TPSFQEECKF RETLLPNNYN AYESDLYQGT YIALSKYGRV KRGSKVSPIM TVTHFLPRI.
Background
What is the molecular weight/Mw of FGF6 Protein?
FGF6 Protein has a total Mw of 18.9kDa.

What is the source or expression system of FGF6 Protein?
Escherichia Coli.

What is the Purity of FGF6 Protein?
FGF6 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF6 Protein?
The biological functionality of FGF6 Protein will be determined in the future.

What is the amino acid sequence of FGF6 Protein?
MGTRANNTLL DSRGWGTLLS RSRAGLAGEI AGVNWESGYL VGIKRQRRLY CNVGIGFHLQ VLPDGRISGT HEENPYSLLE ISTVERGVVS LFGVRSALFV AMNSKGRLYA TPSFQEECKF RETLLPNNYN AYESDLYQGT YIALSKYGRV KRGSKVSPIM TVTHFLPRI.

What applications can FGF6 Protein be used in?
FGF6 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF6 Protein?
The endotoxin level is minimal, FGF6 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:

Connective Tissue Growth Factor Human Recombinant , HEK

CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF.

Product # :

CYT-687

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Quantity :

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Description

The CTGF Human Recombinant produced in HEK293 cells, is 36kDa protein containing a total of 329 amino acid residues (aa 27-349) including a C-terminal 6×His tag.

Source

HEK293 cells.

Formulation

CTGF filtered (0.2µm) solution in 0.1M Citrate buffer pH 4.7 and 20% (w/v) glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Connective Tissue Growth Factor belongs to the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 (Cystein rich 61), CTGF (Connective Tissue Growth Factor), Nov (Nephroblastoma Overexpressed gene), WISP-1, 2 and 3 (Wnt-1 Induced Secreted Proteins). The CCN genes encode secreted proteins associated with the Extracellular Matrix (ECM) and cell membrane.
CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: fibrosis, vascular ailments and tumorigenesis.
Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes.
The full length protein consists of four modules: Module I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins (IGFBPs).
Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat (VWC).
Module III contains sequences sharing identity with the Thrombospondin type 1 repeat (TSP1) (WSXCSXXCG), which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion.
Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand's factor and mucins. Sequence similarities to heparin-binding motifs are also found within this domain.
Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy.
In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells.
CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.
Synonyms
CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF.
Physical Appearance
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
QNCSGPCRCP DEPAPRCPAG VSLVLDGCGC CRVCAKQLGE LCTERDPCDP HKGLFCHFGS PANRKIGVCT AKDGAPCIFG GTVYRSGESF QSSCKYQCTC LDGAVGCMPL CSMDVRLPSP DCPFPRRVKL PGKCCEEWVC DEPKDQTVVG PALAAYRLED TFGPDPTMIR ANCLVQTTEW SACSKTCGMG ISTRVTNDNA SCRLEKQSRL CMVRPCEADL EENIKKGKKC IRTPKISKPI KFELSGCTSM KTYRAKFCGV CTDGRCCTPH RTTTLPVEFK CPDGEVMKKN MMFIKTCACH YNCPGDNDIF ESLYYRKMYG DMA HHHHHH.
Background
What is the molecular weight/Mw of CTGF Protein?
CTGF Protein has a total Mw of 36kDa.

What is the source or expression system of CTGF Protein?
HEK293 cells.

What is the Purity of CTGF Protein?
CTGF Protein is >90% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of CTGF Protein?
QNCSGPCRCP DEPAPRCPAG VSLVLDGCGC CRVCAKQLGE LCTERDPCDP HKGLFCHFGS PANRKIGVCT AKDGAPCIFG GTVYRSGESF QSSCKYQCTC LDGAVGCMPL CSMDVRLPSP DCPFPRRVKL PGKCCEEWVC DEPKDQTVVG PALAAYRLED TFGPDPTMIR ANCLVQTTEW SACSKTCGMG ISTRVTNDNA SCRLEKQSRL CMVRPCEADL EENIKKGKKC IRTPKISKPI KFELSGCTSM KTYRAKFCGV CTDGRCCTPH RTTTLPVEFK CPDGEVMKKN MMFIKTCACH YNCPGDNDIF ESLYYRKMYG DMA HHHHHH.

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

What is the endotoxin level for CTGF Protein?
The endotoxin level is minimal, CTGF 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 Human Recombinant

Urogastrone, URG, EGF.

Product # :

CYT-217

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Epidermal Growth Factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6.2kDa. The EGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

EGF was lyophilized from a concentrated (1mg/ml) solution containing PBS pH-7.4.

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 0.1 ng/ml, corresponding to a specific activity of >1.0x10⁷ IU/mg.

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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 Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution 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 Epidermal 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
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR.
Background
About EGF:
In the sphere of biomedical studies, epidermal boom factor (EGF) is a cornerstone that gives precious insights into the mechanisms underlying tissue healing, differentiation, and mobile proliferation. In this article we will explore the characteristics and uses of epidermal growth factor (EGF).
Description:
Epidermal growth factor (EGF) is a 6-kDa protein consisting of 53 amino acid residues and 3 intramolecular disulfide linkages. Human tissues, such as platelets, the parotid gland, and the submandibular gland, are rich in EGF. EGF, which was first discovered in human urine and the submaxillary glands of mice, functions as a major modulator of cell proliferation by attaching to its receptor, EGFR, which is found on the cell membrane. EGF triggers autophosphorylation of transmembrane protein tyrosine kinase EGFR upon binding, hence initiating downstream signaling cascades through pathways such as phosphatidylinositol and ras. Beyond the cell membrane, EGF has a variety of roles as it also initiates cytoplasmic processes such actin depolymerization and membrane ruffle formation. Studies indicate that EGF and its receptor might possibly be important components of the nucleus, highlighting the complexity of EGF-mediated cellular responses.
Function:
By attaching to the epidermal growth factor receptor (EGFR), EGF promotes the survival, differentiation, and multiplication of cells. This connection is essential for boosting many physiological processes and stimulating cell proliferation. The preservation of oro-esophageal and stomach tissue integrity is greatly supported by salivary EGF, which is regulated by dietary inorganic iodine. Its actions include the healing of gastric and oral ulcers, the inhibition of gastric acid secretion, the stimulation of DNA synthesis, and the protection of mucosal surfaces against harmful substances such as bile acids, gastric acid, and bacteria. Salivary EGF's role extends to repairing gastric tissue and addressing oro-esophagal issues, showcasing its healing ability in resolving oral and gastrointestinal ailments, including ulcers.
Mechanism:
EGF functions by forming a strong bond with the cell surface's epidermal growth factor receptor (EGFR), which triggers ligand- induced dimerization. This incident sets off the intrinsic protein-tyrosine kinase activity of EGFR, which in turn initiates a signal transduction cascade inside the cell. Numerous biochemical changes are brought about by this cascade, such as increased intracellular calcium levels, increased glycolysis and protein synthesis, and increased expression of particular genes, most notably the EGFR gene. These carefully planned alterations eventually promote DNA synthesis and cell division, illuminating the complex process by which EGF directs basic biological functions and modulates cellular responses.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6.2kDa.

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

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

What is the Biological Activity of EGF Protein?
The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 0.1 ng/ml, corresponding to a specific activity of >1.0x107 IU/mg.

What is the amino acid sequence of EGF Protein?
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR.

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

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

Granulocyte-Colony Stimulating Factor Pegylated Human Recombinant

CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

Product # :

CYT-018

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Quantity :

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Shipped with Ice Packs

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Description

Granulocyte Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8kDa. The Pegylated G-CSF is produced by attaching a 20kDa methoxypolyethylene glycol propionaldehyde (mPEG-ALD) to the N-terminal amino acid of G-CSF giving a total molecular mass of 38.8kDa. G-CSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

G-CSF is supplied in solution (0.69mg/ml) containing 10mM Acetate Buffer (pH 4.0), and 0.004% Polysorbate 80.

Purity

Greater than 95.0% as determined by SEC-HPLC.

Biological Activity

The ED₅₀, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

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Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene. 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. This csf induces granulocytes.
Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Physical Appearance
Colorless, clear and transparent solution.
Stability
G-CSF PEG should be stored refrigerated at 2° to 8°C. Vials should be kept in theirpackaging to protect from light until the time of use. Shaking and freezing should be avoided.
Background
What is the molecular weight/Mw of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein has a total Mw of 18.8kDa.

What is the source or expression system of G CSF HUMAN, PEG Protein?
Escherichia Coli.

What is the Purity of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of G CSF HUMAN, PEG Protein?
The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

What is the amino acid sequence of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein is composed from 175 amino acids.

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

What is the endotoxin level for G CSF HUMAN, PEG Protein?
The endotoxin level is minimal, G CSF HUMAN, PEG 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:

Growth differentiation factor 10 Human Recombinant

Bone morphogenetic protein 3b, BMP-3b, Growth/differentiation factor 10, GDF-10, Bone-inducing protein, BIP, GDF10, BMP3B.

Product # :

CYT-659

Price :

Quantity :

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sds-page

Description

GDF10 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids (369-478 a.a.) and having a total molecular mass of 12.5 kDa. GDF10 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GDF10 solution (1mg/ml) contains 10mM Sodium citrate (pH 3.5), 1mM DTT, 40% glycerol and 0.1M NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

sds-page

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Introduction
GDF10 is a member of the BMP family and the TGF-beta superfamily. GDF10 is expressed in femur, brain, lung, skeletal, muscle, pancreas and testis, and has a role in head formation and possibly multiple roles in skeletal morphogenesis. In humans, GDF10 mRNA is found in the cochlea and lung of fetuses, and in testis, retina, pineal gland, and other neural tissues of adults. The BMP family members are regulators of cell growth and differentiation in both embryonic and adult tissues. These proteins are characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing 7 conserved cysteine residues.
Synonyms
Bone morphogenetic protein 3b, BMP-3b, Growth/differentiation factor 10, GDF-10, Bone-inducing protein, BIP, GDF10, BMP3B.
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
MQWDEPRVCS RRYLKVDFAD IGWNEWIISP KSFDAYYCAG ACEFPMPKIV RPSNHATIQS IVRAVGIIPG IPEPCCVPDK MNSLGVLFLD ENRNVVLKVY PNMSVDTCAC R.
Background
What is the molecular weight/Mw of GDF10 HUMAN Protein?
GDF10 HUMAN Protein has a total Mw of 12.5kDa.

What is the source or expression system of GDF10 HUMAN Protein?
Escherichia Coli.

What is the Purity of GDF10 HUMAN Protein?
GDF10 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF10 HUMAN Protein?
The biological functionality of GDF10 HUMAN Protein will be determined in the future.

What is the amino acid sequence of GDF10 HUMAN Protein?
MQWDEPRVCS RRYLKVDFAD IGWNEWIISP KSFDAYYCAG ACEFPMPKIV RPSNHATIQS IVRAVGIIPG IPEPCCVPDK MNSLGVLFLD ENRNVVLKVY PNMSVDTCAC R.

What applications can GDF10 HUMAN Protein be used in?
GDF10 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDF10 HUMAN Protein?
The endotoxin level is minimal, GDF10 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:

Fibroblast Growth Factor-21 Human Recombinant, His Tag

Fibroblast growth factor 21, FGF-21.

Product # :

CYT-281

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Quantity :

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Shipped with Ice Packs

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source
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Description

Fibroblast Growth Factor -21 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 202 amino acids (29-209) and having a molecular mass of 21.6 kDa (molecular weight on SDS-PAGE will appear higher). The FGF-21 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The FGF-21 His tag protein (1mg/ml) solution in 20mM Tris-HCl buffer pH-8 and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
The FGFs are a family of more than 20 small (~17–26 kDa) secreted peptides. The initial characterization of these proteins focused on their ability to stimulate fibroblast proliferation. This mitogenic activity was mediated through FGF receptors (FGFRs) 1, 2, or 3. A fourth closely related tyrosine kinase receptor (FGFR4) was able to bind the FGFs but did not lead to a mitogenic response.
FGFs modulate cellular activity via at least 5 distinct subfamilies of high-affinity FGF receptors (FGFRs): FGFR-1, -2, -3, and -4, all with intrinsic tyrosine kinase activity and, except for FGFR-4, multiple splice isoforms, and FGFR-5, which lacks an intracellular kinase domain. There is growing evidence that FGFRs can be important for regulation of glucose and lipid homeostasis. The overexpression of a dominant negative form of FGFR-1 in ? cells leads to diabetes in mice, which thus implies that proper FGF signaling is required for normal ? cell function and glycemia maintenance. FGFR-2 appears to be a key molecule during pancreatic development. Moreover, FGFR-4 has been implicated in cholesterol metabolism and bile acid synthesis.
FGF-19, has been shown to cause resistance to diet-induced obesity and insulin desensitization and to improve insulin, glucose, and lipid profiles in diabetic rodents. Since these effects, at least in part, are mediated through the observed changes in metabolic rates, FGF-19 can be considered as a regulator of energy expenditure.
FGF-21 is preferentially expressed in liver, but an exact knowledge of FGF-21 bioactivity and its mode of action have been lacking to date. FGF-21 is a potent activator of glucose uptake on adipocytes, protects animals from diet-induced obesity when overexpressed in transgenic mice, and lowers blood glucose and triglyceride levels when therapeutically administered to diabetic rodents.
Synonyms
Fibroblast growth factor 21, FGF-21.
Physical Appearance
Sterile Filtered colorless 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 MHPIPDSSPL LQFGGQVRQR YLYTDDAQQT EAHLEIREDG TVGGAADQSP ESLLQLKALK PGVIQILGVKTSRFLCQRPD GALYGSLHFD PEACSFRELL LEDGYNVYQS EAHGLPLHLP GNKSPHRDPA PRGPARFLPL PGLPPAPPEP PGILAPQPPD VGSSDPLSMV GPSQGRSPSY AS.
Background
What is the molecular weight/Mw of FGF21,HIS Protein?
FGF21,HIS Protein has a total Mw of 21.6kDa.

What is the source or expression system of FGF21,HIS Protein?
Escherichia Coli.

What is the Purity of FGF21,HIS Protein?
FGF21,HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF21,HIS Protein?
The biological functionality of FGF21,HIS Protein will be determined in the future.

What is the amino acid sequence of FGF21,HIS Protein?
MGSSHHHHHH SSGLVPRGSH MHPIPDSSPL LQFGGQVRQR YLYTDDAQQT EAHLEIREDG TVGGAADQSP ESLLQLKALK PGVIQILGVKTSRFLCQRPD GALYGSLHFD PEACSFRELL LEDGYNVYQS EAHGLPLHLP GNKSPHRDPA PRGPARFLPL PGLPPAPPEP PGILAPQPPD VGSSDPLSMV GPSQGRSPSY AS.

What applications can FGF21,HIS Protein be used in?
FGF21,HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF21,HIS Protein?
The endotoxin level is minimal, FGF21,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:

Myostatin Propeptide Human Recombinant, HEK

GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

Product # :

CYT-936

Price :

Quantity :

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source
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Description

Myostatin Propetide Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asn24-Arg266) containing a total of 253 amino acids, having a calculated molecular mass of 29.1kDa. Myostatin Propetide is fused to a 10 aa C-terminal His tag.

Source

HEK 293.

Formulation

Myostatin Propetide solution at a concentration of 0.25mg/ml in phosphate buffered saline (PBS) pH 8.0 and 20% (w/v) glycerol.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
GDF8 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.
Synonyms
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
Physical Appearance
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
NENSEQKENV EKEGLCNACT WRQNTKSSRI EAIKIQILSK LRLETAPNIS KDVIRQLLPK APPLRELIDQ YDVQRDDSSD GSLEDDDYHA TTETIITMPT ESDFLMQVDG KPKCCFFKFS SKIQYNKVVK AQLWIYLRPV ETPTTVFVQI LRLIKPMKDG TRYTGIRSLK LDMNPGTGIW QSIDVKTVLQ NWLKQPESNL GIEIKALDEN GHDLAVTFPG PGEDGLNPFL EVKVTDTPKR SRR HHHHHHH HHH.

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 (1-51 a.a.)Human Recombinant

Urogastrone, URG, EGF.

Product # :

CYT-1115

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Epidermal Growth Factor (1-51 a.a.) Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 51 amino acids and having a molecular mass of 6.0kDa. The EGF is purified by proprietary chromatographic techniques.

Source

Saccharomyces cerevisiae

Formulation

Lyophilized from a 0.2μm filtered concentrated 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 is determined by a cell proliferation assay using murine Balb/c 3T3 cells and is < than 0.1 ng/ml, corresponding to a specific activity of > 1.0 × 10⁷ IU/mg.

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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 several 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 EGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Epidermal Growth Factor 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 Epidermal 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
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E.
Background
Exploring the Potential of Epidermal Growth Factor (1-51 a.a.) Human Recombinant: Novel Insights and Therapeutic Prospects
Abstract:
Epidermal Growth Factor (EGF) stands as a pivotal cytokine orchestrating essential cellular processes. This concise research paper delves into the unique realm of Epidermal Growth Factor (1-51 a.a.) Human Recombinant, unveiling its intricate molecular dynamics, signaling cascades, and therapeutic promise. Employing cutting-edge methodologies encompassing in vitro assays and animal models, this study elucidates the multifaceted cellular responses sparked by this truncated EGF variant, paving the way for potential clinical applications.
Introduction:
The truncated form of EGF, spanning amino acids 1 to 51 (a.a.), carries distinct attributes that set it apart from the full-length counterpart. This paper centers on exploring the intriguing dimensions of Epidermal Growth Factor (1-51 a.a.) Human Recombinant, offering new insights into its interactions and potential utility.
Molecular Insights and Signaling Dynamics:
At the heart of its function lies the interplay between EGF (1-51 a.a.) and the epidermal growth factor receptor (EGFR). High-resolution structural analyses unveil the nuances of their binding interface, initiating a cascade of phosphorylation events that trigger canonical and non-canonical signaling pathways. The MAPK pathway and the PI3K/Akt pathway, intricately modulated by EGF (1-51 a.a.), propel cellular processes like proliferation, migration, and evasion of apoptosis.
In Vitro Profiling and Cellular Responses:
In dissecting the cellular responses, diverse in vitro assays have been employed. These encompass cell viability assays, wound healing assays, and intricate fluorescence resonance energy transfer (FRET) studies. These assays converge to illuminate the dynamic orchestration of EGF-induced cellular behaviors, showcasing its role in promoting cellular migration, division, and wound closure.
In Vivo Implications and Therapeutic Horizons:
Translating these insights into tangible therapeutic possibilities, in vivo studies present a compelling narrative. In animal models, EGF (1-51 a.a.) emerges as a potent player in cutaneous wound healing, fostering accelerated tissue regeneration. Moreover, its potential extends to oncology, as it not only influences tumor microenvironments but also demonstrates anti-apoptotic effects, hinting at its role in tailored cancer interventions.
Future Prospects and Challenges:
While these discoveries hold immense promise, challenges persist. The intricate network of signaling events demands further scrutiny, considering potential cross-talk and off-target effects. Refining delivery mechanisms and dosing regimens is essential for realizing the clinical potential of EGF (1-51 a.a.).
Conclusion:
In a synthesis of complex molecular insights and tangible therapeutic potential, Epidermal Growth Factor (1-51 a.a.) Human Recombinant emerges as a captivating subject. Its truncated structure and distinctive signaling cascades paint a canvas of cellular orchestration. As research advances, harnessing its therapeutic benefits could usher in novel interventions for wound healing and cancer therapy.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6kDa.

What is the source or expression system of EGF Protein?
Saccharomyces cerevisiae

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

What is the Biological Activity of EGF Protein?
The ED50 is determined by a cell proliferation assay using murine Balb/c 3T3 cells and is < than 0.1 ng/ml, corresponding to a specific activity of > 1.0 × 107 IU/mg.

What is the amino acid sequence of EGF Protein?
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E.

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

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

Cell Growth Regulator With EF-Hand Domain 1 Human Recombinant

Cell Growth Regulator With EF-Hand Domain 1, Cell Growth Regulatory Gene 11 Protein, Hydrophobestin, CGR11, Cell Growth Regulator With EF Hand Domain Protein 1, Cell Growth Regulator With EF Hand Domain 1, Cell growth regulator with EF hand domain protein 1.

Product # :

PRO-2154

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Description

CGREF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 305 amino acids (20-301 a.a) and having a molecular mass of 32.3kDa. CGREF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CGREF1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH7.4).

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Cell Growth Regulator with EF-Hand Domain 1, also known as CGREF1 is a secreted calcium ion binding protein. CGREF1 includes two EF-hand domains & both EF-hands are essential for function. CGREF1 is most likely digested extracellularly by an unfamiliar serine protease generating extremely hydrophobic bioactive peptides. CGREF1 mediates cell-cell adhesion in a calcium-dependent manner. In addition, CGREF1 is capable to inhibit growth in more than a few cell lines.
Synonyms
Cell Growth Regulator With EF-Hand Domain 1, Cell Growth Regulatory Gene 11 Protein, Hydrophobestin, CGR11, Cell Growth Regulator With EF Hand Domain Protein 1, Cell Growth Regulator With EF Hand Domain 1, Cell growth regulator with EF hand domain protein 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 MGSAPKDGVT RPDSEVQHQL LPNPFQPGQE QLGLLQSYLK GLGRTEVQLE HLSREQVLLY LFALHDYDQS GQLDGLELLS MLTAALAPGA ANSPTTNPVI LIVDKVLETQ DLNGDGLMTP AELINFPGVA LRHVEPGEPL APSPQEPQAV GRQSLLAKSP LRQETQEAPG PREEAKGQVE ARRESLDPVQ EPGGQAEADG DVPGPRGEAE GQAEAKGDAP GPRGEAGGQA EAEGDAPGPR GEAGGQAEAR ENGEEAKELP GETLESKNTQ NDFEVHIVQV ENDEI.

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-13 Human Recombinant

Growth Differentiation Factor 6, Growth/Differentiation Factor 16, Bone Morphogenetic Protein 13, BMP-13, BMP13, GDF-6, Klippel-Feil Malformation, Segmentation Syndrome 1, Klip-Feil Malformation, Klippel-Feil Syndrome, MCOPCB6, SCDO4, CDMP2, LCA17, MCOP4, GDF16, KFS1, KFSL, SGM1, KFM, KFS, GDF6.

Product # :

CYT-938

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

BMP13 Human Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 120 amino acids and having a molecular mass of 27.1kDa.The BMP-13 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BMP-13 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

Purity

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

Biological Activity

The ED₅₀ as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 2.0µg/ml, corresponding to a specific activity of > 500IU/mg.

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Introduction
Growth/differentiation factors (GDF1-GDF15) belong to the BMP family of TGF-beta superfamily proteins. These factors are produced as inactive preproproteins which are subsequently cleaved and assembled into active secreted homodimers. BMP13 is a growth factor which controls proliferation and cellular differentiation in the retina and bone formation. BMP13 has a central role in regulating apoptosis during retinal development. GDF proteins are vital during embryonic development, particularly in the skeletal, nervous, and muscular systems. BMP13 gene mutations result in colobomata, which are congenital abnormalities in ocular development, and in Klippel-Feil syndrome (KFS), which is a congenital disorder of spinal segmentation.
Synonyms
Growth Differentiation Factor 6, Growth/Differentiation Factor 16, Bone Morphogenetic Protein 13, BMP-13, BMP13, GDF-6, Klippel-Feil Malformation, Segmentation Syndrome 1, Klip-Feil Malformation, Klippel-Feil Syndrome, MCOPCB6, SCDO4, CDMP2, LCA17, MCOP4, GDF16, KFS1, KFSL, SGM1, KFM, KFS, GDF6.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BMP13 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-13 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 BMP13 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TAFASRHGKR HGKKSRLRCS KKPLHVNFKE LGWDDWIIAP LEYEAYHCEG VCDFPLRSHL EPTNHAIIQT LMNSMDPGST PPSCCVPTKL TPISILYIDA GNNVVYKQYE DMVVESCGCR.
Background
Bone Morphogenetic Protein-13 Human Recombinant: Unraveling its Potential in Tissue Engineering and Regenerative Medicine
Abstract:
Bone Morphogenetic Protein-13 (BMP-13) human recombinant is a pivotal member of the bone morphogenetic protein family, known for its crucial role in tissue development, regeneration, and repair. This research paper aims to provide a comprehensive analysis of BMP-13, including its characteristics, signaling pathways, and potential therapeutic applications. Furthermore, innovative methodologies for the production and optimization of BMP-13 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 in addressing tissue repair and regeneration challenges. BMP-13, a prominent member of the BMP family, plays a vital role in orchestrating cellular responses during tissue development and healing. This paper explores the distinctive features of BMP-13 and presents novel approaches for the production and optimization of BMP-13 human recombinant, aiming to unlock its therapeutic potential in various regenerative contexts.
Characteristics and Signaling Pathways:
BMP-13 is a secreted growth factor belonging to the transforming growth factor-beta (TGF-β) superfamily. It exerts its biological effects by binding to specific cell surface receptors, initiating intricate intracellular signaling cascades. BMP-13 signaling pathways, including Smad-dependent and Smad-independent pathways, regulate critical processes such as cell differentiation, proliferation, and extracellular matrix synthesis, influencing tissue development and repair.
Production of BMP-13 Human Recombinant:
Efficient production methodologies are crucial for harnessing the therapeutic potential of BMP-13 human recombinant. Various recombinant protein expression systems, such as mammalian cells or baculovirus-insect cell systems, have been utilized for the production of functional BMP-13. Optimization strategies, including codon optimization, signal peptide engineering, and protein folding enhancement, have been employed to improve the yield and bioactivity of BMP-13 recombinant protein.
Potential Therapeutic Applications:
BMP-13 human recombinant holds immense promise in the field of tissue engineering and regenerative medicine. Its involvement in cartilage formation, osteogenesis, and tissue repair makes it a potential candidate for the treatment of musculoskeletal disorders, joint injuries, and cartilage defects. Furthermore, the ability of BMP-13 to modulate cell behavior and tissue remodeling indicates its wider therapeutic applications in diverse regenerative processes.
Conclusion:
BMP-13 human recombinant emerges as a crucial regulator in tissue engineering and regenerative medicine, offering significant potential for tissue repair and regeneration. Optimizing production methodologies and further unraveling its signaling mechanisms will undoubtedly enhance its therapeutic applications. Given its involvement in cartilage and bone formation, as well as tissue repair, BMP-13 human recombinant represents a valuable tool for promoting tissue regeneration and addressing the unmet clinical needs in regenerative medicine.
What is the molecular weight/Mw of GDF6 Protein?
GDF6 Protein has a total Mw of 27.1kDa.

What is the source or expression system of GDF6 Protein?
Escherichia Coli.

What is the Purity of GDF6 Protein?
GDF6 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF6 Protein?
The ED50 as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 2.0µg/ml, corresponding to a specific activity of > 500IU/mg.

What is the amino acid sequence of GDF6 Protein?
TAFASRHGKR HGKKSRLRCS KKPLHVNFKE LGWDDWIIAP LEYEAYHCEG VCDFPLRSHL EPTNHAIIQT LMNSMDPGST PPSCCVPTKL TPISILYIDA GNNVVYKQYE DMVVESCGCR.

What applications can GDF6 Protein be used in?
GDF6 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDF6 Protein?
The endotoxin level is minimal, GDF6 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:

Amphiregulin Human Recombinant

Schwannoma-derived growth factor, Colorectum cell-derived growth factor, AR, CRDGF, SDGF, AREGB, MGC13647.

Product # :

CYT-041

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
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Description

Amphiregulin (AREG) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 98 amino acids and having a molecular mass of 11.3 KDa.The AREG is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4.

Purity

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

Biological Activity

Determined by its ability to stimulate the proliferation of mouse Balb/c 3T3 cells. The expected ED₅₀ for this effect is 5-10 ng/ml, corresponding to a specific activity of 100,000-200,000units/mg.

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Synonyms
Schwannoma-derived growth factor, Colorectum cell-derived growth factor, AR, CRDGF, SDGF, AREGB, MGC13647.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized AREG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution AREG 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 AREG in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SVRVEQVVKP PQNKTESENT SDKPKRKKKG GKNGKNRRNR KKKNPCNAEF QNFCIHGECK YIEHLEAVTC KCQQEYFGER CGEKSMKTHS MIDSSLSK.
Background
Amphiregulin Human Recombinant: Exploring its Role in Cancer Biology and Therapeutic Applications
Abstract:

Amphiregulin, a member of the epidermal growth factor (EGF) family, has gained significant attention in cancer research. This research paper provides an overview of Amphiregulin human recombinant, highlighting its molecular characteristics, signaling pathways, and therapeutic potential. Understanding the multifaceted role of Amphiregulin opens avenues for targeted cancer therapies. This article provides a concise analysis of Amphiregulin, emphasizing its impact on cancer biology and its therapeutic applications.
Introduction:

Cancer continues to be a significant health challenge worldwide, necessitating novel therapeutic approaches. Amphiregulin, an EGF family member, has emerged as a promising target in cancer research. This paper provides an overview of Amphiregulin, shedding light on its structure, function, and therapeutic potential.
Amphiregulin Signaling and Mechanisms:

Amphiregulin exerts its effects through the binding and activation of the EGF receptor (EGFR). Upon activation, a cascade of intracellular signaling pathways is triggered, including the MAPK and PI3K/AKT pathways. These pathways regulate critical cellular processes such as cell proliferation, survival, migration, and angiogenesis.
Amphiregulin in Cancer Biology:

Amphiregulin has been implicated in various aspects of cancer biology, including tumor growth, metastasis, and resistance to therapy. Its overexpression is observed in several cancer types, and its role in promoting tumor growth and metastasis has been demonstrated in preclinical studies. Targeting Amphiregulin signaling shows promise in inhibiting cancer progression and overcoming therapy resistance.
Therapeutic Potential of Amphiregulin Human Recombinant:

Amphiregulin human recombinant holds significant therapeutic potential in cancer treatment. Strategies aimed at blocking Amphiregulin-EGFR interactions or inhibiting downstream signaling pathways are being explored as potential therapeutic interventions. Additionally, Amphiregulin could serve as a predictive biomarker to identify patients who are more likely to respond to targeted therapies.
Challenges and Future Directions:

While the therapeutic targeting of Amphiregulin shows promise, several challenges need to be addressed. Further research is required to fully understand the complex interplay between Amphiregulin and other molecular pathways in cancer biology. Additionally, the development of specific and potent inhibitors and the identification of patient selection criteria are important considerations for successful clinical translation.
Conclusion:

Amphiregulin human recombinant represents a promising avenue for targeted cancer therapy. Understanding the molecular mechanisms and functional implications of Amphiregulin in cancer biology offers new opportunities for developing innovative treatments. Continued research in this field has the potential to improve patient outcomes and contribute to the advancement of personalized medicine.
What is the molecular weight/Mw of AREG Protein?
AREG Protein has a total Mw of 11.3kDa.

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

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

What is the Biological Activity of AREG Protein?
Determined by its ability to stimulate the proliferation of mouse Balb/c 3T3 cells. The expected ED50 for this effect is 5-10 ng/ml, corresponding to a specific activity of 100,000-200,000units/mg.

What is the amino acid sequence of AREG Protein?
SVRVEQVVKP PQNKTESENT SDKPKRKKKG GKNGKNRRNR KKKNPCNAEF QNFCIHGECK YIEHLEAVTC KCQQEYFGER CGEKSMKTHS MIDSSLSK.

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

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

Prolactin-Induced Protein Human Recombinant

Prolactin-inducible protein, Gross cystic disease fluid protein 15, GCDFP-15, Prolactin-induced protein, Secretory actin-binding protein, SABP, gp17, GCDFP15, GPIP4, PIP.

Product # :

CYT-793

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Shipped with Ice Packs

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Description

PIP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 141 amino acids (29-146 a.a.) and having a molecular mass of 15.9kDa.PIP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Prolactin-inducible protein (PIP) is a main protein component of benign breast gross cysts. PIP is a famous indicator of breast cancer, since it is found in around 50% of all breast cancer specimens. PIP is expressed in exocrine glands, in pathologic conditions, in breast cysts and breast cancers exhibiting apocrine features. PIP and prostate specific antigen are co-expressed in androgen receptor-positive breast tumours.
Synonyms
Prolactin-inducible protein, Gross cystic disease fluid protein 15, GCDFP-15, Prolactin-induced protein, Secretory actin-binding protein, SABP, gp17, GCDFP15, GPIP4, PIP.
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 MGSQDNTRKI IIKNFDIPKS VRPNDEVTAV LAVQTELKEC MVVKTYLISS IPLQGAFNYK YTACLCDDNP KTFYWDFYTN RTVQIAAVVD VIRELGICPD DAAVIPIKNN RFYTIEILKV E.

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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