Search: 1000 results found for "Insulin-Like Growth Factor"

Description:

IGF-1 Rat Recombinant

Somatomedin C, IGF-I, IGFIA, IGF1.

Product # :

CYT-289

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Description

IGF-1 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7.7kDa. IGF-I is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized with a 0.2µm filtered concentrated solution in 20mM PBS, pH 7.0.

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by a cell proliferation assay using FDC-P1 cells is less than 2.0ng/ml, corresponding to a specific activity of >500,000units/mg.

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Introduction
The somatomedins, or IGFs, comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of GH. Early studies showed that GH 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, IGFIA, IGF1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IGF-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGFI 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 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GPETLCGAEL VDALQFVCGP RGFYFNKPTG YGSSIRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPTKSA.

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 Binding Protein-1 Human Recombinant, HEK

IBP-1, IGF-Binding Protein 1, AFBP, PP12, IGF-BP25, hIGFBP-1, IGFBP-1.

Product # :

CYT-1214

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Description

IGFBP1 Human Recombinant is a single, glycosylated, polypeptide chain (26-259 a.a) containing a total of 234 amino acids, having a molecular mass of 25.2 kDa. IGFBP1 is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The IGFBP1 solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50 is ≤3 ug/ml, measured by its ability to inhibit proliferation using MCF-7 human breast cancer cells in the presence of Human IGF-1.

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Synonyms
IBP-1, IGF-Binding Protein 1, AFBP, PP12, IGF-BP25, hIGFBP-1, IGFBP-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
APWQCAPCSA EKLALCPPVS ASCSEVTRSA GCGCCPMCAL PLGAACGVAT ARCARGLSCR ALPGEQQPLH ALTRGQGACV QESDASAPHA AEAGSPESPE STEITEEELL DNFHLMAPSE EDHSILWDAI STYDGSKALH VTNIKKWKEP CRIELYRVVE SLAKAQETSG EEISKFYLPN CNKNGFYHSR QCETSMDGEA GLCWCVYPWN GKRIPGSPEI RGDPNCQIYF NVQN.
Background
IGFBP-1 (Insulin-like Growth Factor Binding Protein-1) is a vital protein that regulates the actions of insulin-like growth factors (IGFs) in various physiological processes. This research paper aims to investigate the structure, function, and potential therapeutic applications of IGFBP-1, shedding light on its diverse roles in growth regulation and its therapeutic potential.
IGFBP-1 belongs to the IGFBP family and is primarily synthesized and secreted by the liver. It acts as a carrier protein, binding to IGFs in the bloodstream and modulating their availability and distribution to target tissues. By binding to IGFs, IGFBP-1 regulates IGF signaling pathways, influencing cellular growth, differentiation, and metabolism.
The structure of IGFBP-1 comprises an N-terminal domain responsible for IGF binding, followed by linker regions and a C-terminal domain involved in protein-protein interactions. Post-translational modifications, including phosphorylation and glycosylation, further regulate the activity and stability of IGFBP-1.
IGFBP-1 plays a pivotal role in modulating IGF actions in various tissues and physiological contexts. It is involved in fetal development, skeletal growth, and tissue repair. Additionally, IGFBP-1 has been implicated in metabolic regulation, insulin sensitivity, and the pathogenesis of metabolic disorders such as diabetes and obesity.
Therapeutically, IGFBP-1 holds significant promise. Its ability to modulate IGF activity opens avenues for targeted therapies in conditions associated with dysregulated IGF signaling, including cancer. The dysregulation of the IGF pathway is frequently observed in cancer, making IGFBP-1 an attractive candidate for novel therapeutic approaches. Manipulating IGFBP-1 levels or developing IGFBP-1-derived peptides may offer innovative strategies for inhibiting tumor growth or enhancing the effectiveness of existing cancer therapies.
The availability of IGFBP-1 human recombinant proteins has greatly facilitated research and development endeavors. Recombinant IGFBP-1 proteins provide invaluable tools for investigating the interactions between IGFBP-1, IGFs, and other regulatory molecules. They enable detailed exploration of the molecular mechanisms underlying IGFBP-1 function and offer opportunities to unlock its full therapeutic potential.

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:

IGF-1 Bovine Recombinant

Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA MGF.

Product # :

CYT-1261

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Description

IGF1 Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7.6kDa. IGF- I is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The IGF1 Bovine was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.0.

Purity

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

Biological Activity

The biological activity was determined by the cell proliferation assay using serum free human MCF-7 cells in <2ng/ml, corresponding to a Specific Activity of >5.0 x 10⁵IU/mg.

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Introduction
The somatomedins, IGFs, comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of GH. Early studies showed that GH 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. Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B.
Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA MGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IGF-1 Bovine although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution bovine IGF1 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 bovine IGF-1 in sterile 18MΩ-cm H2O at a concentration of 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-1, Mouse Anti-Human

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

Product # :

ANT-062

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Formulation

1mg/ml in PBS (after reconstitution).

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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.
Solubility
Reconstitute with of H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human Growth Hormone
Ig Subclass
Mouse IgM
Clone
NYRhIGF1
Applications
Direct ELISA, Western Blot, Immuneprecipitation.
Titer
By direct ELISA, 1:10,000 dilution will yield 0.5 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
Type
Mouse Anti Human Monoclonal.
Storage Procedures
Lyophilized: store at 4°C. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
Purification Method
Boric acid precipitation

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:

IGF-2 Human Recombinant

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

Product # :

CYT-265

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Description

Insulin-Like Growth Factor- II Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 67 amino acids and having a molecular mass of 7.5k Dalton. IGF-II is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a sterile filtered solution containing 0.1 % trifluoroacetic acid (TFA).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The activity is determined by the dose dependent proliferation of FDC-P1 cells and is typically 8.39ng/mL corresponding to a specific activity of 1.2x10⁵units/mg..

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Introduction
IGF-2 is a member of the INS family of polypeptide growth factors that is involved in development and growth. It is an imprinted gene and is expressed only from the paternally inherited allele. It is a candidate gene for eating disorders. There is a read-through, INS-IGF2, which aligns to this gene at the 3' region and to the upstream INS gene at the 5' region. Two alternatively spliced transcript variants encoding the same protein have been found for this gene.
Synonyms
Somatomedin-A, IGF2, INSIGF, pp9974, C11orf43, FLJ22066, FLJ44734.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IGF-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGFII 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 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AYRPSETLCG GELVDTLQFV CGDRGFYFSR PASRVSRRSR 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:

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:

IGF1 Gilthead Seabream Recombinant

Somatomedin C, IGF-I, IGFI.

Product # :

CYT-295

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Description

IGF1 Gilthead SeabreamRecombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 68 amino acids and having a molecular mass of 7545.4 Dalton, the predicted pI=7.72.IGF-1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

Purity

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

Biological Activity

Binding assays of the 125I-Gealthead Seabream IGF1 to Gilthead Seabream or carp (Cyprinus carpio) sera resulted in high specific binding, indicating the existence of one or more IGF-binding proteins. In binding experiments to crude Gilthead Seabream brain homogenate, using human (h) IGF-I as a ligand, the respective IC50 value of hIGF1 was about fourfold lower than that of Gilthead Seabream IGF-1. Recombinant Gilthead Seabream IGF-1 exhibited mitogenic activity in a mouse mammary gland-derived MME-L1 cell line which was approximately 200-fold lower than that of hIGF1. Binding experiments to intact MME-L1 cells suggests that this difference most likely results from a correspondingly lower affinity for IGF1 receptor in these cells. In contrast, the activities of Gilthead Seabream IGF-I and hIGF-I measured by 35S uptake by gill arches from the goldfish (Carassius auratus) were identical, indicating that the recombinant Gilthead Seabream IGF-I is biologically active.

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Introduction
The somatomedins, or IGFs, comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of GH. Early studies showed that GH 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. Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2), and somatomedin B.
Synonyms
Somatomedin C, IGF-I, IGFI.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IGF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 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 IGF-1 in sterile 0.4% NaHCO3 adjusted to ph 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSPETLCGAELVDTLQFVCGERGFYFSKPGYGPNARRSRGIVDECCFQSCELRRLEMYCAPAKTSK
Protein content
Somatomedin C quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.60 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of IGF1 as a Reference Standard.

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:

IGFBP-6 Human Recombinant

IGFBP-6, IBP-6, IGF-binding protein 6.

Product # :

CYT-258

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Description

IGFBP6 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing amino acids 148-240 and having a molecular mass of 20 kDa including 4kDa His tag. IGFBP6 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IBP-6 was lyophilized from a concentrated (1mg/ml) solution containing 1xPBS, 0.1% SDS and 1mM DTT.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
IGFBP6 plays a role in lipoprotein assembly and dietary cholesterol absorption. in addition to its acyltransferase activity, it may act as a ligase. may provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa.
Synonyms
IGFBP-6, IBP-6, IGF-binding protein 6.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IBP6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGFBP-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 IGFBP6 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:

Insulin Like Growth Factor Binding Protein-3 Human Recombinant, His Tag

Insulin-like growth factor-binding protein 3, Insulin Like Growth Factor Binding Protein-3, His Tag, IGFBP3, IBP-3, IGF-binding protein 3, IGFBP-3, IBP3, BP-53, Insulin-like growth factor binding protein 3 isoform b precursor.

Product # :

CYT-879

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Shipped with Ice Packs

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Description

IGFBP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 285 amino acids (28-291a.a.) and having a molecular mass of 31kDa.IGFBP3 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IGFBP3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

Purity

Greater than 90.0% as determined by analysis by SDS-PAGE.

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Introduction
IGFBP3 is a member of the insulin-like growth factor binding protein (IGFBP) family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein forms a ternary complex with insulin-like growth factor acid-labile subunit (IGFALS) and either insulin-like growth factor (IGF) I or II. In this form, it circulates in the plasma, prolonging the half-life of IGFs and altering their interaction with cell surface receptors. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
Synonyms
Insulin-like growth factor-binding protein 3, Insulin Like Growth Factor Binding Protein-3, His Tag, IGFBP3, IBP-3, IGF-binding protein 3, IGFBP-3, IBP3, BP-53, Insulin-like growth factor binding protein 3 isoform b precursor.
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 MGASSAGLGP VVRCEPCDAR ALAQCAPPPA VCAELVREPG CGCCLTCALS EGQPCGIYTE RCGSGLRCQP SPDEARPLQA LLDGRGLCVN ASAVSRLRAY LLPAPPAPGN ASESEEDRSA GSVESPSVSS THRVSDPKFH PLHSKIIIIK KGHAKDSQRY KVDYESQSTD TQNFSSESKR ETEYGPCRRE MEDTLNHLKF LNVLSPRGVH IPNCDKKGFY KKKQCRPSKG RKRGFCWCVD KYGQPLPGYT TKGKEDVHCY SMQSK.

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 Human Recombinant

Product # :

CYT-270

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Quantity :

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Shipped at Room temp

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Description

Insulin Human Recombinant produced in E.Coli is a two chain, non-glycosylated polypeptide chain containing 51 amino acids and having a molecular mass of 5807 Dalton. Insulin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.

Purity

Greater than 98.0% as determined by RP-HPLC analysis.

Biological Activity

The Biological Activity was determined to be 28 units/mg.

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Introduction
Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Insulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Insulin 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 Insulin in sterile 0.005N HCl not more than 1 mg/ml.

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

Description:

Cysteine-Rich Angiogenic Inducer 61 Human Recombinant

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

Product # :

CYT-164

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Description

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

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

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

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Introduction
CYR61 is a growth factor-inducible, immediate-early gene that has multifaceted activities in various cancers. CYR61 is a secreted, cysteine-rich, binding protein which is encoded by a growth factor-inducible immediate-early gene. Acting as an extracellular, matrix-associated signaling molecule, CYR61 promotes the adhesion of endothelial cells through interaction with integrin and enhances growth factor-induced DNA synthesis in the same cell type.
Synonyms
CYR61, Protein CYR61, Cysteine-rich angiogenic inducer 61, IGF-binding protein 10, IGFBP-10, IBP-10, Protein GIG1, CCN family member 1, CCN1, GIG1, IGFBP10.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CYR61 Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CYR61 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized CYR61 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TCPAACHCPL EAPKCAPGVG LVRDGCGCCK VCAKQLNEDC SKTQPCDHTK GLECNFGASS TALKGICRAQ SEGRPCEYNS RIYQNGESFQ PNCKHQCTCI DGAVGCIPLC PQELSLPNLG CPNPRLVKVT GQCCEEWVCD EDSIKDPMED QDGLLGKELG FDASEVELTR NNELIAVGKG SSLKRLPVFG MEPRILYNPL QGQKCIVQTT SWSQCSKTCG TGISTRVTND NPECRLVKET RICEVRPCGQ PVYSSLKKGK KCSKTKKSPE PVRFTYAGCL SVKKYRPKYC GSCVDGRCCT
PQLTRTVKMR FRCEDGETFS KNVMMIQSCK CNYNCPHANE AAFPFYRLFN DIHKFRD
Background
Title: Cysteine-Rich Angiogenic Inducer 61 Human Recombinant: A Potential Regulator of Angiogenesis
Abstract:

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

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

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

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

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

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

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

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

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

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

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

What is the endotoxin level for CCN1 Protein?
The endotoxin level is minimal, CCN1 Protein was purified using conventional chromatography techniques.

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

Description:

Insulin (20-110 a.a) Human Recombinant

Product # :

CYT-1237

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Description

The Insulin Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The Insulin His-Tagged Fusion Protein, produced in E. coli, is a 13kDa protein containing 91 amino acid residues of the Insulin Human, 20-110 amino acids.

Source

Escherichia Coli.

Formulation

Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized Insulin 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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Amino Acid Sequence
MALWMRLLPL LALLALWGPD PAAAFVNQHL CGSHLVEALY LVCGERGFFY TPKTRREAED LQVGQVELGG GPGAGSLQPL ALEGSLQKRG IVEQCCTSIC SLYQLENYCN
Background
Insulin participates in the metabolism of carbohydrates, proteins and fats by regulating glucose homeostasis in the body. Insulin decreases blood glucose concentration. Insulin hormone facilitates the uptake of glucose into cells, mainly in muscle and fat tissues, and stimulates the liver to store glucose as glycogen. Insulin also inhibits the production of gluconeogenesis and promotes the synthesis of proteins and lipids. Insulin increases cell permeability to monosaccharides, fatty acids and amino acids. Insulin accelerates glycolysis, the pentose phosphate cycle and glycogen synthesis in liver.

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:

Hepatoma Derived Growth Factor-Like 1 Human Recombinant

Hepatoma-derived growth factor-like protein 1, DJ309H15.1, PWWP1, PWWP domain-containing protein 1.

Product # :

CYT-850

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Description

HDGFL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 274 amino acids (1-251 a.a) and having a molecular mass of 29.6kDa.HDGFL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

HDGFL1 protein solution (0.25mg/ml) containing Phosphate buffered saline, (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Hepatoma Derived Growth Factor-Like 1 (HDGFL1) is a member of the HDGF family and contains 1 PWWP domain.
Synonyms
Hepatoma-derived growth factor-like protein 1, DJ309H15.1, PWWP1, PWWP domain-containing protein 1.
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 MGSMSAYGMP MYKSGDLVFA KLKGYAHWPA RIEHMTQPNR YQVFFFGTHE TAFLSPKRLF PYKECKEKFG KPNKRRGFSA GLWEIENNPT VQASDCPLAS EKGSGDGPWP EPEAAEGDED KPTHAGGGGD ELGKPDDDKP TEEEKGPLKR SAGDPPEDAP KRPKEAAPDQ EEEAEAERAA EAERAAAAAA ATAVDEESPF LVAVENGSAP SEPGLVCEPP QPEEEELREE EVADEEASQE WHAEAPGGGD RDSL.
Background
What is the molecular weight/Mw of HDGFL1 HUMAN Protein?
HDGFL1 HUMAN Protein has a total Mw of 29.6kDa.

What is the source or expression system of HDGFL1 HUMAN Protein?
Escherichia Coli.

What is the Purity of HDGFL1 HUMAN Protein?
HDGFL1 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of HDGFL1 HUMAN Protein?
The biological functionality of HDGFL1 HUMAN Protein will be determined in the future.

What is the amino acid sequence of HDGFL1 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSMSAYGMP MYKSGDLVFA KLKGYAHWPA RIEHMTQPNR YQVFFFGTHE TAFLSPKRLF PYKECKEKFG KPNKRRGFSA GLWEIENNPT VQASDCPLAS EKGSGDGPWP EPEAAEGDED KPTHAGGGGD ELGKPDDDKP TEEEKGPLKR SAGDPPEDAP KRPKEAAPDQ EEEAEAERAA EAERAAAAAA ATAVDEESPF LVAVENGSAP SEPGLVCEPP QPEEEELREE EVADEEASQE WHAEAPGGGD RDSL.

What applications can HDGFL1 HUMAN Protein be used in?
HDGFL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for HDGFL1 HUMAN Protein?
The endotoxin level is minimal, HDGFL1 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:

Hepatoma-Derived Growth Factor (32-285 a.a) Human Recombinant

Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF, DFNB39.

Product # :

CYT-294

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SDS-PAGE

Description

HGF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 255 amino acids (32-285 a.a.) and having a molecular mass of 29.8kDa. HGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 80% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
Hepatocyte Growth Factor (HGF) is a multifunctional growth factor which regulates both cell growth and cell motility. It exerts a strong mitogenic effect on hepatocytes and primary epithelial cells. HGF synergizes with Interleukin-3 and GM-CSF to stimulate colony formation of hematopoietic progenitor cells in vitro and may, therefore, also modulate hematopoiesis.
Synonyms
Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF, DFNB39.
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
MQRKRRNTIH EFKKSAKTTL IKIDPALKIK TKKVNTADQC ANRCTRNKGL PFTCKAFVFD KARKQCLWFP FNSMSSGVKK EFGHEFDLYE NKDYIRNCII GKGRSYKGTV SITKSGIKCQ PWSSMIPHEH SYRGKDLQEN YCRNPRGEEG GPWCFTSNPE VRYEVCDIPQ CSEVECMTCN GESYRGLMDH TESGKICQRW DHQTPHRHKF LPERYPDKGF DDNYCRNPDG QPRPWCYTLD PHTRWEYCAI KTCET.
Background
What is the molecular weight/Mw of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein has a total Mw of 29.8kDa.

What is the source or expression system of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
Escherichia Coli.

What is the Purity of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein is >80% pure as determined by SDS-PAGE.

What is the Biological Activity of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
What is the molecular weight/Mw of HGF (32-285) HUMAN Protein? HGF (32-285) HUMAN Protein has a total Mw of 29.8kDa. What is the source or expression system of HGF (32-285) HUMAN Protein? Escherichia Coli. What is the Purity of HGF (32-285) HUMAN Protein? HGF (32-285) HUMAN Protein is >80% pure as determined by SDS-PAGE. What is the Biological Activity of HGF (32-285) HUMAN Protein? The biological functionality of HGF (32-285) HUMAN Protein will be determined in the future. What is the amino acid sequence of HGF (32-285) HUMAN Protein? MQRKRRNTIH EFKKSAKTTL IKIDPALKIK TKKVNTADQC ANRCTRNKGL PFTCKAFVFD KARKQCLWFP FNSMSSGVKK EFGHEFDLYE NKDYIRNCII GKGRSYKGTV SITKSGIKCQ PWSSMIPHEH SYRGKDLQEN YCRNPRGEEG GPWCFTSNPE VRYEVCDIPQ CSEVECMTCN GESYRGLMDH TESGKICQRW DHQTPHRHKF LPERYPDKGF DDNYCRNPDG QPRPWCYTLD PHTRWEYCAI KTCET. What applications can HGF (32-285) HUMAN Protein be used in? HGF (32-285) HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow. What is the endotoxin level for HGF (32-285) HUMAN Protein? The endotoxin level is minimal, HGF (32-285) HUMAN Protein was purified using conventional chromatography techniques.

What is the amino acid sequence of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
MQRKRRNTIH EFKKSAKTTL IKIDPALKIK TKKVNTADQC ANRCTRNKGL PFTCKAFVFD KARKQCLWFP FNSMSSGVKK EFGHEFDLYE NKDYIRNCII GKGRSYKGTV SITKSGIKCQ PWSSMIPHEH SYRGKDLQEN YCRNPRGEEG GPWCFTSNPE VRYEVCDIPQ CSEVECMTCN GESYRGLMDH TESGKICQRW DHQTPHRHKF LPERYPDKGF DDNYCRNPDG QPRPWCYTLD PHTRWEYCAI KTCET.

What applications can HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein be used in?
HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
The endotoxin level is minimal, HEPATOCYTE GROWTH FACTOR (32-285) 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:

Nephroblastoma Overexpressed Human Recombinant

Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.

Product # :

CYT-805

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Description

Nephroblastoma Overexpressed Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 331 amino acids and having a molecular mass of 36.2 kDa. The NOV is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris-HCl, pH 8.6 and 150 mM NaCl.

Purity

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

Biological Activity

Determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 µg/ml, corresponding to a specific activity of > 1000 IU/mg. range of 10.0 -50.0 ng/ml, corresponding to a specific activity of 20,000-100,000units/mg.

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Introduction
Nephroblastoma Overexpressed (NOV) which is encoded by the NOV gene is a part of the CCN (CTGF/CYR61/NOV) family. NOV takes part in reducing tumorgenicity and proliferation of certain cancer cell lines. NOV interacts with numerous proteins and is involved in both internal and external cell signaling. NOV is expressed in particular tumors, including Wilm’s tumor and most nephroblastomas and is also exerts proangiogenic activities.
Synonyms
Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized NOV although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NOV 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 NOV in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MQVAATQRCP PQCPGRCPAT PPTCAPGVRA VLDGCSCCLV CARQRGESCS DLEPCDESSG LYCDRSADPS NQTGICTAVE GDNCVFDGVI YRSGEKFQPS CKFQCTCRDG QIGCVPRCQL DVLLPEPNCP APRKVEVPGE CCEKWICGPD EEDSLGGLTL AAYRPEATLG VEVSDSSVNC IEQTTEWTAC SKSCGMGFST RVTNRNRQCE MLKQTRLCMV RPCEQEPEQP TDKKGKKCLR TKKSLKAIHL QFKNCTSLHT YKPRFCGVCS DGRCCTPHNT KTIQAEFQCS PGQIVKKPVM VIGTCTCHTN CPKNNEAFLQ ELELKTTRGK M.

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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Shipped at Room temp

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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:

Insulin Receptor Human Recombinant

Insulin receptor, IR, EC 2.7.10.1, CD220, INSR, HHF5.

Product # :

CYT-777

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Shipped at Room temp

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Description

Insulin Receptor Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (aa 28-944 of the short isoform- HIR-A, Uniprot accession # P06213-2 which includes the whole subunit alpha and extracellular domain of subunit beta) containing a total of 927 amino acids, having a molecular mass of 105.9kDa (calculated), though it migrates at approximately 160kDa on SDS PAGE, the INSR is fused to a 2 a.a N-terminal linker, a 2 a.a C-terminal linker and fused to a 6 a.a His tag at C-Terminus.The Human INSR is purified by proprietary chromatographic techniques.

Source

HEK 293.

Formulation

INSR was filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Insulin Receptor (INSR) is a receptor tyrosine kinase which mediates the pleiotropic actions of insulin. Binding of insulin to the insulin receptor (INSR) stimulates glucose uptake. Once the precursor signal peptide is removed, the insulin receptor precursor is post-translationally cleaved into 2 chains (alpha and beta) which are covalently linked. Insulin binding initiates phosphorylation of several intracellular substrates, including, insulin receptor substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL and other signaling intermediates. Each of these phosphorylated proteins function as docking proteins for other signaling proteins which contain Src-homology-2 domains (SH2 domain) that specifically recognize different phosphotyrosines residues, including the p85 regulatory subunit of PI3K and SHP2.
Synonyms
Insulin receptor, IR, EC 2.7.10.1, CD220, INSR, HHF5.
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.
Solubility
It is recommended to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. INSR is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
ASHLYPGEVC PGMDIRNNLT RLHELENCSV IEGHLQILLM FKTRPEDFRD LSFPKLIMIT DYLLLFRVYG LESLKDLFPN LTVIRGSRLF FNYALVIFEM VHLKELGLYN LMNITRGSVR IEKNNELCYL ATIDWSRILD SVEDNYIVLN KDDNEECGDI CPGTAKGKTN CPATVINGQF VERCWTHSHC QKVCPTICKS HGCTAEGLCC HSECLGNCSQ PDDPTKCVAC RNFYLDGRCV ETCPPPYYHF QDWRCVNFSF CQDLHHKCKN SRRQGCHQYV IHNNKCIPEC PSGYTMNSSN LLCTPCLGPC PKVCHLLEGE KTIDSVTSAQ ELRGCTVING SLIINIRGGN NLAAELEANL GLIEEISGYL KIRRSYALVS LSFFRKLRLI RGETLEIGNY SFYALDNQNL RQLWDWSKHN LTITQGKLFF HYNPKLCLSE IHKMEEVSGT KGRQERNDIA LKTNGDQASC ENELLKFSYI RTSFDKILLR WEPYWPPDFR DLLGFMLFYK EAPYQNVTEF DGQDACGSNS WTVVDIDPPL RSNDPKSQNH PGWLMRGLKP WTQYAIFVKT LVTFSDERRT YGAKSDIIYV QTDATNPSVP LDPISVSNSS SQIILKWKPP SDPNGNITHY LVFWERQAED SELFELDYCL KGLKLPSRTW SPPFESEDSQ KHNQSEYEDS AGECCSCPKT DSQILKELEE SSFRKTFEDY LHNVVFVPRP SRKRRSLGDV GNVTVAVPTV AAFPNTSSTS VPTSPEEHRP FEKVVNKESL VISGLRHFTG YRIELQACNQ DTPEERCSVA AYVSARTMPE AKADDIVGPV THEIFENNVV HLMWQEPKEP NGLIVLYEVS YRRYGDEELH LCVSRKHFAL ERGCRLRGLS PGNYSVRIRA TSLAGNGSWT EPTYFYVTDY LDVPSNIAKK LHHHHHH.

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-18 Human Recombinant, His Tag

Fibroblast growth factor 18, FGF-18, zFGF5, FGF18.

Product # :

CYT-935

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Description

FGF18 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Glu28-Ala207) containing 190 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 22.3kDa.

Source

Escherichia Coli.

Formulation

FGF18 was filtered (0.4µm) and lyophilized in phosphate buffered saline and 5% w/v trehalose.

Purity

Purity as determined by densitometric image analysis is greater than 95%.

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Introduction
Fibroblast growth factor 18 (FGF18) is a member of the large FGF family which has at least 23 members. FGF18 is a binding growth factor with a core 120 amino acid FGF domain which allows for a common tertiary structure. FGFs are expressed in the course of the embryonic development and in restricted adult tissues. FGF-18 is an indispensable regulator of long bone and calvarial development. FGF-18 signals via FGFR 1c, 2c, 3c, and 4.
Synonyms
Fibroblast growth factor 18, FGF-18, zFGF5, FGF18.
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. FGF18 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHASEENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQPELQK PFKYTTVTKR SRRIRPTHPA.
Background
What is the molecular weight/Mw of FGF18 HIS Protein?
FGF18 HIS Protein has a total Mw of 22.3kDa.

What is the source or expression system of FGF18 HIS Protein?
Escherichia Coli.

What is the Purity of FGF18 HIS Protein?
FGF18 HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF18 HIS Protein?
The biological functionality of FGF18 HIS Protein will be determined in the future.

What is the amino acid sequence of FGF18 HIS Protein?
MKHHHHHHASEENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQPELQK PFKYTTVTKR SRRIRPTHPA.

What applications can FGF18 HIS Protein be used in?
FGF18 HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF18 HIS Protein?
The endotoxin level is minimal, FGF18 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:

Fibroblast Growth Factor Basic 147 a.a. Human Recombinant

Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.

Product # :

CYT-557

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Description

Fibroblast Growth Factor-2 Human Recombinant (FGF-2) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 147 amino acids and having a molecular mass of 16.5kDa. The FGF2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The bFGF was lyophilized from a sterile filtered solution containing 20mM Tris-HCl, pH 7.6 and 150mM NaCl.

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, Calculated by the dose- dependent proliferation of mouse BALB/c 3T3 cells is < 0.05ng/ml corresponding to a specific activity of 2.0x10⁷ units/mg.

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Introduction
FGF-basic is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.
Synonyms
Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized basic-FGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGFb 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 FGF-B in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MPALPEDGGS GAFPPGHFKD PKRLYCKNGG FFLRIHPDGR VDGVREKSDP HIKLQLQAEE RGVVSIKGVC ANRYLAMKED GRLLASKCVT DECFFFERLE SNNYNTYRSR KYTSWYVALK RTGQYKLGSK TGPGQKAILF LPMSAKS.
Background
What is the molecular weight/Mw of FGF 2 Protein?
FGF 2 Protein has a total Mw of 16.5kDa.

What is the source or expression system of FGF 2 Protein?
Escherichia Coli.

What is the Purity of FGF 2 Protein?
FGF 2 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF 2 Protein?
The ED50, Calculated by the dose- dependent proliferation of mouse BALB/c 3T3 cells is < 0.05ng/ml corresponding to a specific activity of 2.0x107 units/mg.

What is the amino acid sequence of FGF 2 Protein?
MPALPEDGGS GAFPPGHFKD PKRLYCKNGG FFLRIHPDGR VDGVREKSDP HIKLQLQAEE RGVVSIKGVC ANRYLAMKED GRLLASKCVT DECFFFERLE SNNYNTYRSR KYTSWYVALK RTGQYKLGSK TGPGQKAILF LPMSAKS.

What applications can FGF 2 Protein be used in?
FGF 2 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF 2 Protein?
The endotoxin level is minimal, FGF 2 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:

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

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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:

Connective Tissue Growth Factor Human Recombinant (182-250 a.a.)

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

Product # :

CYT-526

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Description

The Connective Tissue Growth Factor amino acids 182-250, produced in E.Coli, is a fusion protein with His Tag (4 kDa), having a total molecular mass of 15 kDa.

Source

Escherichia Coli.

Formulation

Lyophilized without any additives.

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 modulesModule 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, Connective Tissue Growth Factor.
Physical Appearance
Sterile Filtered white lyophilized 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 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Background
What is the molecular weight/Mw of CTGF Protein?
CTGF Protein has a total Mw of 15kDa.

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?
The biological functionality of CTGF Protein will be determined in the future.

What is the amino acid sequence of CTGF Protein?
CTGF Protein is composed from 180-250 amino acids.

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:

Transforming Growth Factor-Beta 3 (24-412 a.a.) Human Recombinant

Transforming Growth Factor, Beta 3, Prepro-Transforming Growth Factor Beta-3, TGF-Beta-3, ARVD1, RNHF, Arrhythmogenic Right Ventricular Dysplasia 1, Transforming Growth Factor Beta-3, TGF-Beta3, ARVD, Transforming growth factor beta-3, TGF-beta-3.

Product # :

CYT-886

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Shipped with Ice Packs

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Description

TGFB3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 412 amino acids (24-412 a.a) and having a molecular mass of 47.2kDa. TGFB3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TGFB3 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. Three TGF Betas have been identified in mammals. TGF Beta 1, TGF Beta 2 and TGF Beta 3 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 3, Prepro-Transforming Growth Factor Beta-3, TGF-Beta-3, ARVD1, RNHF, Arrhythmogenic Right Ventricular Dysplasia 1, Transforming Growth Factor Beta-3, TGF-Beta3, ARVD, Transforming growth factor beta-3, TGF-beta-3.
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 MGSLSTCTTL DFGHIKKKRV EAIRGQILSK LRLTSPPEPT VMTHVPYQVL ALYNSTRELL EEMHGEREEG CTQENTESEY YAKEIHKFDM IQGLAEHNEL AVCPKGITSK VFRFNVSSVE KNRTNLFRAE FRVLRVPNPS SKRNEQRIEL FQILRPDEHI AKQRYIGGKN LPTRGTAEWL SFDVTDTVRE WLLRRESNLG LEISIHCPCH TFQPNGDILE NIHEVMEIKF KGVDNEDDHG RGDLGRLKKQ KDHHNPHLIL MMIPPHRLDN PGQGGQRKKR ALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSADTTHST VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS.

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:

Hepatoma-Derived Growth Factor-2 Human Recombinant

Hepatoma-derived growth factor-related protein 3, HRP-3, Hepatoma-derived growth factor 2, HDGF-2, HDGFRP3, HDGF2, CGI-142.

Product # :

CYT-132

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SDS-PAGE

Description

HDGF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (1-203 a.a.) and having a molecular mass of 25.1kDa (Molecular weight on SDS-PAGE will appear higher). HDGF2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

HDGF2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

Purity

Greater than 90% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
Hepatoma-derived growth factor, related protein 3 (HDGFRP3/HDGF2) is the original member of a family of polypeptides labeled HDGF related proteins (HRPs). The HDGF2 protein augments DNA synthesis and may play a part in cell proliferation. HDGF2 is expressed primarily in the testis and the brain, to an intermediate extent in the heart, and to a slight extent in the ovaries, kidneys, spleen, and liver in humans.
Synonyms
Hepatoma-derived growth factor-related protein 3, HRP-3, Hepatoma-derived growth factor 2, HDGF-2, HDGFRP3, HDGF2, CGI-142.
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 MGSHMARPRP REYKAGDLVF AKMKGYPHWP ARIDELPEGA VKPPANKYPI FFFGTHETAF LGPKDLFPYK EYKDKFGKSN KRKGFNEGLW EIENNPGVKF TGYQAIQQQS SSETEGEGGN TADASSEEEG DRVEEDGKGK RKNEKAGSKR KKSYTSKKSS
KQSRKSPGDE DDKDCKEEEN KSSSEGGDAG NDTRNTTSDL QKTSEGT.
Background
What is the molecular weight/Mw of HDGF2 HUMAN Protein?
HDGF2 HUMAN Protein has a total Mw of 25.1kDa.

What is the source or expression system of HDGF2 HUMAN Protein?
Escherichia Coli.

What is the Purity of HDGF2 HUMAN Protein?
HDGF2 HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of HDGF2 HUMAN Protein?
The biological functionality of HDGF2 HUMAN Protein will be determined in the future.

What is the amino acid sequence of HDGF2 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMARPRP REYKAGDLVF AKMKGYPHWP ARIDELPEGA VKPPANKYPI FFFGTHETAF LGPKDLFPYK EYKDKFGKSN KRKGFNEGLW EIENNPGVKF TGYQAIQQQS SSETEGEGGN TADASSEEEG DRVEEDGKGK RKNEKAGSKR KKSYTSKKSS
KQSRKSPGDE DDKDCKEEEN KSSSEGGDAG NDTRNTTSDL QKTSEGT.

What applications can HDGF2 HUMAN Protein be used in?
HDGF2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for HDGF2 HUMAN Protein?
The endotoxin level is minimal, HDGF2 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:

ProInsulin C-Peptide Analogue Human Recombinant

Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.

Product # :

CYT-1120

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

ProInsulin C-Peptide Analogue Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 35 amino acid and having a molecular mass of approximately 3.6kDa.ProInsulin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

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Introduction
Insulin decreases blood glucose concentration. Insulin increases cell permeability to monosaccharides, amino acids and fatty acids. Insulin accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
Synonyms
Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized ProInsulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ProInsulin C-Peptide Analogue 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 ProInsulin C-Peptide Analogue in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
RREAEDLQVG QVELGGGPGA GSLQPLALEG SLQKR.

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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