Search: 1000 results found for "angiogenin"

Description:

Calbindin-2 Mouse Recombinant

Calretinin, CR, Calb2, calbindin 2.

Product # :

PRO-290

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
More Info
Citations

Description

Calretinin Mouse Recombinant full length protein expressed in E.coli, shows a 57 kDa band on SDS-PAGE.The Calretinin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Calretinin protein at 100µg/ml in 50mM Tris-HCl, pH7.5 and 10mM L-glutathione (reduced).

More Info

Introduction
Calretinin is an intracellular calcium-binding protein belonging to the troponin C superfamily characterized by a structural motif described as the EF-hand domain. The immunohistochemical detection of calretinin in developing cerebellum is restricted to the later stages indicated by weak staining from week 21 of gestation, in Purkinje and basket cells and in neurons of the dentate nucleus. The intensity of staining increases as the cerebellum matures. In tumors, calretinin has been detected in mesotheliomas and some pulmonary adenocarcinomas.
Synonyms
Calretinin, CR, Calb2, calbindin 2.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent freeze-thaw cycles.

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

Description:

Serum Amyloid A (APO-SAA) Equine Recombinant

Product # :

CYT-1222

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info
Citations

Description

SAA Equine produced in E.coli is a single, non-glycosylated polypeptide chain (1-110 a.a) containing 120 a.a and having a molecular mass of 13,580 Dalton. SAA s fused with a 10 amino acids affinity tag at N-Terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SAA was lyophilized from 0.01M HCl (pH 2.0).

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SAA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Serum Amyloid A (APO-SAA) 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 SAA in 0.01M HCl (pH 2.0) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
Elevated SAA levels serve as sensitive markers for various inflammatory disorders, including infections, autoimmune diseases, and cancer. SAA assays, often utilizing recombinant SAA proteins, are invaluable in clinical diagnostics, aiding in disease monitoring and treatment evaluation. Moreover, the targeted modulation of SAA activities presents novel therapeutic strategies, offering potential interventions in conditions characterized by excessive inflammation.
SAA Recombinant Protein, as a representative of the intricate SAA family, embodies the complexities of inflammation, immune regulation, and lipid metabolism. Its versatile roles in health and disease underscore its significance in biology and medicine. By unraveling the molecular intricacies of SAA, scientists pave the way for innovative diagnostic methods, therapeutic interventions, and a deeper understanding of the intricate interplay between inflammation and various physiological processes. This research not only illuminates the multifaceted nature of SAA but also holds the promise of transformative advancements in both clinical practice and scientific discovery.

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:

Tesamorelin

Product # :

HOR-062

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
formulation
purity
More Info
Citations

Description

Tesamorelin is a synthetic single, non-glycosylated polypeptide chain containing 44 amino acids, having a molecular mass of 5135.78 Dalton and a Molecular formula of C221H366N72O67S.

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 97.0% as determined by analysis by RP-HPLC.

More Info

Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Tesamorelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Tesamorelin 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 Tesamorelin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
trans-3-hexenoyl-Tyr-Ala-Asp-Ala-IlePhe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala-Arg-LysLeu-Leu-Gln-Asp-Ile-Met-Ser-Arg-Gln-Gln-Gly-Glu-Ser-Asn-Gln-GluArg-Gly-Ala-Arg-Ala-Arg-Leu-NH2.
Background
Tesamorelin is a growth hormone-releasing hormone (GHRH) analogue. Tesamorelin stimulates the pituitary gland to produce endogenous growth hormone, which targets visceral adipose tissue. Tesamorelin has evolved from a HIV treatment into an effective metabolic and regenerative therapy.

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:

Nectin Cell Adhesion Molecule 3 Human Recombinant

Nectin-3, CDw113, Nectin cell adhesion molecule 3, Poliovirus receptor-related protein 3, CD113, PVRL3, PRR3, NECTIN-3, PVRR3, PPR3.

Product # :

PRO-2504

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

NECTIN3 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 355 amino acids (58-404 a.a.) and having a molecular mass of 39.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).NECTIN3 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

NECTIN3 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4), 20% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
NECTIN3, also known as Nectin Cell Adhesion Molecule 3, is part of the nectin family. NECTIN3 is intended to initiate cell-cell adhesion to stimulate cell attachment and to allow subsequent formation of JAM-and cadherin-based intercellular junctions. NECTIN3 induces endocytosis-mediated down-regulation of PVR from the cell surface, which results in reduction of cell movement & proliferation. Following Nectin-3 activity adds strength to the junction through trans-interaction with various molecules.
Synonyms
Nectin-3, CDw113, Nectin cell adhesion molecule 3, Poliovirus receptor-related protein 3, CD113, PVRL3, PRR3, NECTIN-3, PVRR3, PPR3.
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
GPIIVEPHVT AVWGKNVSLK CLIEVNETIT QISWEKIHGK SSQTVAVHHP QYGFSVQGEY QGRVLFKNYS LNDATITLHN IGFSDSGKYI CKAVTFPLGN AQSSTTVTVL VEPTVSLIKG PDSLIDGGNE TVAAICIAAT GKPVAHIDWE GDLGEMESTT TSFPNETATI ISQYKLFPTR FARGRRITCV VKHPALEKDI RYSFILDIQY APEVSVTGYD GNWFVGRKGV NLKCNADANP PPFKSVWSRL DGQWPDGLLA SDNTLHFVHP LTFNYSGVYI CKVTNSLGQR SDQKVIYISD PPTTTTLQPT IQWHPSTADI EDLATEPKKL PFPLSTLATI KDDTIATLEH HHHHH.

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-2 Human Recombinant, HEK

BMP-2, BMP2A.

Product # :

CYT-080

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

BMP-2 Human Recombinant produced in HEK cells is a glycosylated disulfide-linked homodimer, having a molecular weight range of 28kDa due to glycosylation. The BMP2 is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

The BMP2 was lyophilized from 0.67mg/ml in 2xPBS + 6% ethanol.

Purity

Greater than 95.0% as determined by analysis by SDS-PAGE.

Biological Activity

The specific activity as determined by the dose dependent induction of alkaline phosphatase production in the ATDC-5 cell line (Mouse chondrogenic cell line) was found to be 6.53ng/ml.

More Info

Introduction
BMP2 belongs to the transforming growth factor-beta (TGFB) superfamily. Bone morphogenic protein induces bone formation. BMP2 is a candidate gene for the autosomal dominant disease of fibrodysplasia (myositis) ossificans progressiva.
Synonyms
BMP-2, BMP2A.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BMP2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-2 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 BMP-2 in sterile 4mM HCl containing 0.1% endotoxin-free recombinant HSA.
Amino Acid Sequence
QAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNST NHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR.
Background
What is the molecular weight/Mw of BMP2 Protein?
BMP2 Protein has a total Mw of 28kDa.

What is the source or expression system of BMP2 Protein?
Hek.

What is the Purity of BMP2 Protein?
BMP2 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BMP2 Protein?
The specific activity as determined by the dose dependent induction of alkaline phosphatase production in the ATDC-5 cell line (Mouse chondrogenic cell line) was found to be 6.53ng/ml.

What is the amino acid sequence of BMP2 Protein?
QAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNST NHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR.

What applications can BMP2 Protein be used in?
BMP2 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BMP2 Protein?
The endotoxin level is minimal, BMP2 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:

Leptin N82K Human Recombinant, Pegylated

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-1107

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

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

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

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

More Info

Introduction
Leptin takes an important part in the regulation of energy balance and body weight control.After entering the circulation, Leptin binds LEPRwhich results in the activation of several major signalling pathways. In the hypothalamus Leptin acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption and also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, regulates pancreatic beta-cell function and insulin secretion and affects innate and adaptive immunity.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Pegylated Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Pegylated Leptin N82K should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Pegylated Leptin in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

Description:

Thromboplastin Bovine

Tissue factor, Coagulation factor III, Thromboplastin, CD142, TF, F3, TFA.

Product # :

PRO-2760

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
More Info
Citations

Description

Thromboplastin bovine native

Source

Bovine Lung.

Formulation

The bovine thromboplastin was lyophilized with no additives.

More Info

Introduction
Tissue factor is well-known as the main cellular initiator of blood coagulation. The Tissue factor gene encodes coagulation factor III which is a cell surface glycoprotein that enables cells to initiate the blood coagulation cascades, and functions as the high-affinity receptor for the coagulation factor VII. Following vessel injury, the Tissue Factor and Factor VIIa complex activates the coagulation protease cascade, which leads to fibrin deposition and activation of platelets. The ensuing complex presents a catalytic event, which is responsible for initiation of the coagulation protease cascades by specific limited proteolysis. Therefore, Tissue factor has a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade. Tissue Factor can also be stimulated by the inflammatory mediators interleukin 1 and TNF, as well as by endotoxin, to appear on monocytes and vascular endothelial cells as a component of cellular immune response.
Tissue factor is the only one in the coagulation pathway for which a congenital deficiency has not been described. Certain levels of Tissue Factor are essential for the maintained viability and growth of endothelium and Tissue Factor-expressing tumor cells. Additionally, abnormal Tissue Factor expression inside the vasculature initiates life threatening thrombosis in various diseases, for example sepsis, atherosclerosis, and cancer. Alternative spliced Tissue Factor expression advances tumor growth, and is linked to increased tumor cell proliferation and angiogenesis in pancreatic cancer.
Synonyms
Tissue factor, Coagulation factor III, Thromboplastin, CD142, TF, F3, TFA.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Bovine Thromboplastin although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Prothrombin 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 Bovine Thromboplastin in sterile 0.9% NaCl

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:

Apolipoprotein A-I Human Recombinant

Apolipoprotein A-I, Apo-AI, ApoA-I, APOA1, MGC117399.

Product # :

CYT-750

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info
Citations

Description

Apolipoprotein A-I Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 243 amino acids and having a molecular mass of 28.1kDa.The APOA1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The APOA1 protein was 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.

More Info

Introduction
APOA1 (Apolipoprotein A-1) is a human protein with a specific role in lipid metabolism being the main protein component of HDL in the plasma. APOA1 promotes cholesterol efflux from tissues to the liver for excretion. Furthermore, APOA1 is a cofactor for LCAT, which is responsible for the formation of most plasma cholesteryl esters. In addition, APOA1 activates spermatozoa motility as part of the SPAP complex. The APOA1 gene is strongly linked with two other apolipoprotein genes on chromosome 11. Defects in the APOA1 gene are linked to HDL deficiency including Tangier disease, and with systemic non-neuropathic amyloidosis. High levels of APOA1 are linked to the manifestation of asthma and atopy.
Synonyms
Apolipoprotein A-I, Apo-AI, ApoA-I, APOA1, MGC117399.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Apolipoprotein A-I although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution APOA1 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 APOA1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
DEPPQSPWD RVKDLATVYV DVLKDSGRDY VSQFEGSALG KQLNLKLLDN WDSVTSTFSK LREQLGPVTQ EFWDNLEKET EGLRQEMSKD LEEVKAKVQP YLDDFQKKWQ EEMELYRQKV EPLRAELQEG ARQKLHELQE KLSPLGEEMR DRARAHVDAL RTHLAPYSDE LRQRLAARLE ALKENGGARL AEYHAKATEH LSTLSEKAKP ALEDLRQGLL PVLESFKVSF LSALEEYTKK LNTQ.
Background
Apolipoprotein A-I Human Recombinant: A Promising Therapeutic Agent for Cardiovascular Diseases
Abstract:

Cardiovascular diseases (CVDs) remain a leading cause of mortality worldwide. Dyslipidemia, characterized by abnormal lipid profiles, is a significant risk factor for the development of CVDs. Apolipoprotein A-I (ApoA-I) is the primary protein component of high-density lipoprotein (HDL), known as the "good cholesterol." ApoA-I plays a crucial role in reverse cholesterol transport, promoting the efflux of cholesterol from peripheral tissues to the liver for elimination. Recombinant ApoA-I offers a potential therapeutic strategy for enhancing HDL functionality and reducing CVD risk. This research paper aims to provide an overview of ApoA-I human recombinant, its production methods, and its therapeutic applications in cardiovascular medicine.
Introduction

Cardiovascular diseases and dyslipidemia
Role of apolipoprotein A-I in reverse cholesterol transport
Potential of ApoA-I human recombinant as a therapeutic agent
Structure and Function of Apolipoprotein A-I

Primary structure and domains of ApoA-I
Functional properties of ApoA-I in reverse cholesterol transport
Interaction with other lipoproteins and cellular receptors
Production of Apolipoprotein A-I Human Recombinant

Expression systems for recombinant ApoA-I
Biotechnological methods for large-scale production
Purification and characterization of recombinant ApoA-I
Therapeutic Applications of Apolipoprotein A-I Human Recombinant

Promotion of reverse cholesterol transport
Anti-inflammatory and antioxidant effects
Enhancement of endothelial function
Cardioprotective effects in animal models
Clinical Trials and Future Perspectives

Phase I and II clinical trials
Challenges and limitations
Future directions and potential therapeutic combinations
Conclusion

Summary of the potential of ApoA-I human recombinant as a therapeutic agent for CVDs
Importance of ongoing research and clinical trials
What is the molecular weight/Mw of APOLIPOPROTEIN A1 Protein?
APOLIPOPROTEIN A1 Protein has a total Mw of 28.1kDa.

What is the source or expression system of APOLIPOPROTEIN A1 Protein?
Escherichia Coli.

What is the Purity of APOLIPOPROTEIN A1 Protein?
APOLIPOPROTEIN A1 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of APOLIPOPROTEIN A1 Protein?
The biological functionality of APOLIPOPROTEIN A1 Protein will be determined in the future.

What is the amino acid sequence of APOLIPOPROTEIN A1 Protein?
DEPPQSPWD RVKDLATVYV DVLKDSGRDY VSQFEGSALG KQLNLKLLDN WDSVTSTFSK LREQLGPVTQ EFWDNLEKET EGLRQEMSKD LEEVKAKVQP YLDDFQKKWQ EEMELYRQKV EPLRAELQEG ARQKLHELQE KLSPLGEEMR DRARAHVDAL RTHLAPYSDE LRQRLAARLE ALKENGGARL AEYHAKATEH LSTLSEKAKP ALEDLRQGLL PVLESFKVSF LSALEEYTKK LNTQ.

What applications can APOLIPOPROTEIN A1 Protein be used in?
APOLIPOPROTEIN A1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for APOLIPOPROTEIN A1 Protein?
The endotoxin level is minimal, APOLIPOPROTEIN A1 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 Receptor Antagonist, S. Active Human Recombinant

Mammotropin, Luteotropic hormone, Luteotropin, PRL.

Product # :

CYT-1253

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

Prolactin Human Receptor Antagonist del 1-9, G129R mutant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids + an additional Ala at n-terminal and having a molecular mass of ~ 22 kDa was modified by additional 12 mutations. The Human Prolactin Receptor Antagonist is purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

The protein was lyophilized from a concentrated (1-2mg/ml) solution with 0.02% -0.03% NaHCO3.

Purity

Greater than 97.0% as determined by:

(a) Analysis by Gel Filtration.

(b) Analysis by SDS-PAGE.

Biological Activity

fully biologically active as evidenced by inhibiting PRLR-induced proliferation of Nb2 cells or Baf3 cells stably transfected with hPRL receptors. It also interacts at 1:1 molar ratio with human prolactin receptor extracellular domain as documented by SEC and SPR (Biacore analysis). It is ~ 100 fold more potent than 1-9 G129R hPRL in Ba/F3 cells and > 1000-fold potent in Nb2 cells.

More Info

Synonyms
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PRLR although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 3 mg/ml and filter sterilization PRLR can be stored at 4C for several weeks. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized PRLR 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
The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Arg-Ser-Gln-Val-Thr
Background
Prolactin is a pituitary hormone which takes part in the stimulation of milk production, salt and water regulation, development, growth and reproduction. The primary step in its action is binding a specific membrane receptor (prolactin receptor) which belongs to the superfamily of class 1 cytokine receptors. PRLR varies in size (short and long forms) with tissue source and species, from ~40 kDa to 100 kDa. The PRL-R consists of at least 3 separate domains: an extracellular region with 5 cysteines which contains the prolactin binding site, a single transmembrane domain and a cytoplasmic region, the length of which appears to influence ligand binding and regulate cellular function.

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:

Adiponectin, Mouse Anti Human

Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

Product # :

ANT-232

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

formulation
More Info
Citations

Formulation

containing PBS, pH-7.4, & 0.1% Sodium Azide

More Info

Introduction
Human Adiponectin is a secreted protein expressed exclusively in differentiated adipocyte (adipokine). Adiponectin contains a modular structure comprising an N-terminal collagenous domain followed by a C-terminal globular domain. APM-1 plays a role in various physiological processes such as energy homeostasis and obesity. Plasma levels of adiponectin are reduced in obese humans, and decreased levels are associated with insulin resistance and hyperinsulinemia.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Physical Appearance
Sterile Filtered solution.
Immunogen
Anti-human adiponectin mAb, is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human adiponectin amino acids 15-244 purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and k light chain.
Clone
P1G12AT.
Applications
Adiponectin antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Recommended dilution range for Western blot analysis is 1:250 ~ 1:1,000. The antibody has the specificity against globular domain of adiponectin. Recommended starting dilution is 1:500.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
Adiponectin antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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

Description:

Pramlintide

Product # :

HOR-300

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
formulation
purity
More Info
Citations

Description

Pramlintide Synthetic is a single, non-glycosylated polypeptide chain containing 37 amino acids, having a molecular mass of 3949.4 Dalton and a Molecular formula of C171H267N51O53S2.

Formulation

The protein was lyophilized with no additives.

Purity

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

More Info

Introduction
Pramlintide acetate is a hormone that is released into the bloodstream, in a similar pattern as insulin. Pramlintide aids in the absorption of glucose by slowing gastric emptying, promoting satiety, and inhibiting inappropriate secretion of glucagon, a catabolic hormone that opposes the effects of insulin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Pramlintide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Pramlintide 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 Pramlintide in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions. The Pramlintide is also soluble in 1% Acetic Acid.
Amino Acid Sequence
KCNTATCATNRLANFLVHSSNNFGPILPPTNVGSNTY-NH2.

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:

Cystatin E/M, BioActive Human Recombinant

Cystatin E/M, cystatin 6, Cystatin M, Cystatin-E, Cysteine proteinase inhibitor.

Product # :

PRO-2633

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

CST6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 142 amino acids (29-149 a.a.) and having a molecular mass of 15.9kDa.CST6 is fused to a 21 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The CST6 solution (0.5mg/1ml) contains 10% glycerol, 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The IC50 value is < 10nM. The inhibitory function of Cystatin 6 on protease activity of papain was measured by a fluorometric assay using Z-FR-AMC at pH 7.5 at 25˚C.

More Info

Introduction
Cystatin E/M or CST6 is part of the cystatin type 2 family. Part of the cystatin type 2 family members can act as cysteine protease inhibitors, whereas cystatin E/M regulates cathepsin B inhibitors and not cathepsin C. cystatin E/M is a protein the when secreted, has an effect on osteogenesis and bone resorption, insulin regulation, response to systemic inflammation & hepatocyte growth factor receptors.
Synonyms
Cystatin E/M, cystatin 6, Cystatin M, Cystatin-E, Cysteine proteinase inhibitor.
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 MRPQERMVGE LRDLSPDDPQ VQKAAQAAVA SYNMGSNSIY YFRDTHIIKA QSQLVAGIKY FLTMEMGSTD CRKTRVTGDH VDLTTCPLAA GAQQEKLRCD FEVLVVPWQN SSQLLKHNCV QM

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:

Actin Filament Associated Protein 1 Human Recombinant

Actin filament-associated protein 1, 110 kDa actin filament-associated protein, AFAP-110, AFAP1, AFAP, Actin Filament Associated Protein 1.

Product # :

PRO-1972

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

AFAP1 Human Recombinant produced in E. coli is a single polypeptide chain containing 360 amino acids (250-588) and having a molecular mass of 39.2 kDa.AFAP1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The AFAP1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 80% as determined by SDS-PAGE.

More Info

Introduction
Actin Filament Associated Protein 1 (AFAP1) is a Src binding partner. AFAP1 is a possible modulator of actin filament integrity in response to cellular signals, and is also playing a role as an adaptor protein by connecting Src family members to actin filaments. AFAP1 takes partin the development and progression of prostate adenocarcinoma by regulating cell-matrix adhesions and migration in the cancer cells.
Synonyms
Actin filament-associated protein 1, 110 kDa actin filament-associated protein, AFAP-110, AFAP1, AFAP, Actin Filament Associated 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 MGCSGPVDSE CPPPPSSPVH KAELEKKLSS ERPSSDGEGV VENGITTCNG KEQVKRKKSS KSEAKGTVSK VTGKKITKII SLGKKKPSTD EQTSSAEEDV PTCGYLNVLS NSRWRERWCR VKDNKLIFHK DRTDLKTHIV SIPLRGCEVI PGLDCKHPLT FRLLRNGQEV AVLEASSSED MGRWIGILLA ETGSSTDPEA LHYDYIDVEM SASVIQTAKQ TFCFMNRRVI SANPYLGGTS NGYAHPSGTA LHYDDVPCIN GSLRGKKPPV ASNGVTGKGK TLSSQPKKAD PAAVVKRTGS NAAQYKYGKN RVEADAKRLQ TKEEELLKRK EALRNRLAQL.

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:

Alpha-2-HS-Glycoprotein Human Recombinant HEK

Alpha-2-HS-glycoprotein, Fetuin-A, Alpha-2-Z-globulin, Ba-alpha-2-glycoprotein, AHSG, FETUA, AHS, A2HS, HSGA, PRO2743.

Product # :

PRO-1644

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info
Citations

Description

AHSG Human Recombinant produced by transfected human cells is a single polypeptide chain containing 357 amino acids (19-367). AHSG is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

AHSG was lyophilized from a 0.2 µM filtered solution of 20mM PB and 150mM NaCl, pH 7.5.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
Fetuin is a liver-produced negative acute phase protein composed of two subunits, the A and B chains.
Fetuin homologs have been identified in several species including rat, sheep, pig, rabbit, guinea pig, cattle, mouse and human. Multiple physiological roles for these homologs have been suggested, including ability to bind to hydroxyapatite crystals and to specifically inhibit the tyrosine kinase (TK) activity of the receptor (IR).
Fetuin-A (alpha2-Heremans-Schmid glycoprotein; AHSG) is an important circulating inhibitor of calcification in vivo, and is downregulated during the acute-phase response.
Sera from patients on long-term dialysis with low AHSG concentrations showed impaired ex-vivo capacity to inhibit CaxPO4 precipitation.
Fetuin may influence the resolution of inflammation by modulating the phagocytosis of apoptotic cells by macrophages.
ASHG blocks TGF-beta-dependent signaling in osteoblastic cells, and mice lacking ASHG display growth plate defects, increased bone formation with age, and enhanced cytokine-dependent osteogenesis.
Synonyms
Alpha-2-HS-glycoprotein, Fetuin-A, Alpha-2-Z-globulin, Ba-alpha-2-glycoprotein, AHSG, FETUA, AHS, A2HS, HSGA, PRO2743.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized AHSG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution AHSG 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 AHSG in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APHGPGLIYRQPNCDDPETEEAALVAIDYINQNLPWGYKHTLNQIDEVKVWPQQPSGELFEIE
IDTLETTCHVLDPTPVARCSVRQLKEHAVEGDCDFQLLKLDGKFSVVYAKCDSSPDSAEDVRK
VCQDCPLLAPLNDTRVVHAAKAALAAFNAQNNGSNFQLEEISRAQLVPLPPSTYVEFTVSGTD
CVAKEATEAAKCNLLAEKQYGFCKATLSEKLGGAEVAVTCTVFQTQPVTSQPQPEGANEAVPTP
VVDPDAPPSPPLGAPGLPPAGSPPDSHVLLAAPPGHQLHRAHYDLRHTFMGVVSLGSPSGEVSH
PRKTRTVVQPSVGAAAGPVVPPCPGRIRHFKVVDHHHHHH.

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:

Sonic HedgeHog (C24II) Human Recombinant

Sonic Hedgehog, MCOPCB5, SMMCI, HLP3, HPE3, Sonic Hedgehog (Drosophila) Homolog, Sonic Hedgehog Homolog (Drosophila), Sonic Hedgehog Homolog, Sonic Hedgehog Protein, TPTPS, HHG-1, HHG1, TPT, SHH (C24II).

Product # :

CYT-888

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

SHH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 176 amino acids (24-197 a.a.) and having a molecular mass of 19.8kDa (The Cys at position 24 has been replaced with 2 Ile).The SHH is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The SHH protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4).

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
Sonic Hedgehog is part of a small group of secreted proteins which are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Human Sonic Hedgehog is 99% homologous to the mouse gene. Sonic HedgeHog is a protein that is vital in guding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which functions in association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is essential for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.
Synonyms
Sonic Hedgehog, MCOPCB5, SMMCI, HLP3, HPE3, Sonic Hedgehog (Drosophila) Homolog, Sonic Hedgehog Homolog (Drosophila), Sonic Hedgehog Homolog, Sonic Hedgehog Protein, TPTPS, HHG-1, HHG1, TPT, SHH (C24II).
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
MIIGPGRGFG KRRHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKISRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRSKYGML ARLAVEAGFD WVYYESKAHI HCSVKAENSV AAKSGG

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:

Developmental Pluripotency Associated 3 Human Recombinant

Developmental pluripotency-associated protein 3, Stella-related protein, DPPA3, STELLAR, STELLA.

Product # :

PRO-1291

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

DPPA3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 182 amino acids (1-159 a.a) and having a molecular mass of 20.2kDa.DPPA3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

DPPA3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Developmental Pluripotency Associated 3 (DPPA3) is a protein which in mice may serve as a maternal factor during the preimplantation stage of development. In mice, the DPPA3 protein has a role in transcriptional repression, cell division, and maintenance of cell pluripotentiality. In humans, related intronless loci are found on chromosomes 14 and X. DPPA3 is expressed in embryonic stem and carcinoma cells. DPPA3 has a low expression in the testis, ovary and thymus. DPPA3 is highly expressed in testicular germ cell tumors.
Synonyms
Developmental pluripotency-associated protein 3, Stella-related protein, DPPA3, STELLAR, STELLA.
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 MGSMDPSQFN PTYIPGSPQM LTEENSRDDS GASQISSETL IKNLSNLTIN ASSESVSPLS EALLRRESVG AAVLREIEDE WLYSRRGVRT LLSVQREKMA RLRYMLLGGV RTHERRPTNK EPKGVKKESR PFKCPCSFCV SNGWDPSENA RIGNQDTKPL QP.

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:

Argininosuccinate Synthase 1 Human Recombinant

ASS, CTLN1, EC 6.3.4.5, ASS1, Argininosuccinate Synthase 1.

Product # :

ENZ-548

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

ASS1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 432 amino acids (1-412 a.a.) and having a molecular mass of 48.6 kDa. The ASS1 is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ASS1 Human 0.5mg/ml solution containing 20mM Tris-HCl pH-8, 0.1M NaCl, 1mM DTT & 20% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
ASS1 is involved in the urea cycle, which is a sequence of chemical reactions that is localized in liver cells. The urea cycle processes excess nitrogen that is generated as the body uses proteins. The surplus nitrogen is used to create a molecule called urea, which is excreted from the body in urine.
Synonyms
ASS, CTLN1, EC 6.3.4.5, ASS1, Argininosuccinate Synthase 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 MSSKGSVVLA YSGGLDTSCI LVWLKEQGYD VIAYLANIGQ KEDFEEARKK ALKLGAKKVF IEDVSREFVE EFIWPAIQSS ALYEDRYLLG TSLARPCIAR KQVEIAQREG AKYVSHGATG KGNDQVRFEL SCYSLAPQIK VIAPWRMPEF YNRFKGRNDL MEYAKQHGIP IPVTPKNPWS MDENLMHISY EAGILENPKN QAPPGLYTKT QDPAKAPNTP DILEIEFKKG VPVKVTNVKD GTTHQTSLEL FMYLNEVAGK HGVGRIDIVE NRFIGMKSRG IYETPAGTIL YHAHLDIEAF TMDREVRKIK QGLGLKFAEL VYTGFWHSPE CEFVRHCIAK SQERVEGKVQ VSVLKGQVYI LGRESPLSLY NEELVSMNVQ GDYEPTDATG FININSLRLK EYHRLQSKVT AK.

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:

Neurotensin Human Recombinant, sf9

Neurotensin/neuromedin N, NTS, Neuromedin N, NN, NmN, NT, NmN-125.

Product # :

PRO-2374

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

NTS Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 134 amino acids (24-148) and having a molecular mass of 15.4kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).NTS is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

NTS protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

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

More Info

Introduction
Neurotensin (NTS) is a common precursor for 2 peptides, neuromedin N and neurotensin. Neurotensin is a secreted tridecapeptide, which is generally distributed throughout the central nervous system, and may serve as a neurotransmitter or a neuromodulator. NTS is involved in dopamine-associated pathophysiological events, in the maintenance of gut structure and function, and in the regulation of fat metabolism. Tissue-specific processing may initiate the formation in some tissues of larger forms of neuromedin N and neurotensin. The large forms may embody more stable peptides which are also biologically active.
Synonyms
Neurotensin/neuromedin N, NTS, Neuromedin N, NN, NmN, NT, NmN-125.
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
ADPSDSEEEM KALEADFLTN MHTSKISKAH VPSWKMTLLN VCSLVNNLNS PAEETGEVHE EELVARRKLP TALDGFSLEA MLTIYQLHKI CHSRAFQHWE LIQEDILDTG NDKNGKEEVI KRKIPYILHH HHHH.

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:

Energy Homeostasis Associated Human Recombinant

Adropin, Energy homeostasis-associated protein, ENHO, C9orf165, UNQ470.

Product # :

PRO-1569

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info
Citations

Description

ENHO Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 34-76) containing 121 amino acids including extra 78 N-terminal amino acids. The total molecular mass is 13.05kDa (calculated).

Source

Escherichia Coli.

Formulation

ENHO filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Energy Homeostasis Associated (ENHO) participates in glucose homeostasis maintenance and lipid metabolism. ENHO is expressed in the liver and the brain. The role of ENHO in obesity or diabetes is studied.
Synonyms
Adropin, Energy homeostasis-associated protein, ENHO, C9orf165, UNQ470.
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. ENHO is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MGGKSNGEKK YIVGFKQGFK SCAKKEDVIS EKGGKLQKCF KYVDAASATL NEKAVEELKK DPSVAYVEED KLFKALTSCHSRSADVDSLS ESSPNSSPGP CPEKAPPPQK PSHEGSYLLQ P.

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 Marrow Stromal Cell Antigen 2 Human Recombinant

Bone marrow stromal cell antigen 2, CD317 antigen, BST-2, HM1.24 antigen, Tetherin, NPC-A-7.

Product # :

CYT-059

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
sds-page
Citations

Description

BST2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 133 amino acids (50-161) and having a molecular mass of 14.8 kDa.The BST2 is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BST2 protein 0.5mg/ml is supplied in 20mM Tris-HCl, pH-8, 0.1M NaCl, 1mM DTT and 20% Glycerol.

Purity

Greater than 80.0% as determined by SDS-PAGE.

sds-page

More Info

Introduction
BST2 takes part in the growth and development of B-cells. The human cellular protein BST2 inhibits retrovirus infection by maintaining the diffusion of virus particles after budding from infected cells. BST2 was originally discovered as an inhibitor to HIV-1 infection in the absence of Vpu, but it is also known to inhibit the release of other viruses such as the Lassa and Marburg virions. In addition, BST2 has a part in B-cell activation in rheumatoid arthritis.
Synonyms
Bone marrow stromal cell antigen 2, CD317 antigen, BST-2, HM1.24 antigen, Tetherin,
NPC-A-7.
Physical Appearance
BST2 is supplied as a 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 MSEACRDGLR AVMECRNVTH LLQQELTEAQ KGFQDVEAQA ATCNHTVMAL MASLDAEKAQ GQKKVEELEG EITTLNHKLQ DASAEVERLR RENQVLSVRI ADKKYYPSSQ DSS
Background
The Impact of Bone Marrow Stromal Cell Antigen 2 Human Recombinant in Regenerative Medicine
Introduction
As regenerative medicine progresses from the realm of imagination to tangible reality, Bone Marrow Stromal Cell Antigen 2 (BST-2) human recombinant surfaces as a noteworthy contributor with the potential to reshape the future of therapeutic practices.
BST-2: The Cellular Virtuoso
BST-2, also identified as CD317, is a recognized participant in cellular processes, specifically within the context of viral response. The introduction of BST-2 human recombinant amplifies this role, revealing potential for dramatic advancements in the sphere of regenerative medicine.
Engineering a Cellular Maestro
Capitalizing on the production capacity of E. coli, we successfully synthesized BST-2 human recombinant. This creation was then subject to thorough in vitro examination, focusing on its potential to govern the complex choreography of cellular proliferation and antiviral responses.
Stepping into the Biological Arena
Following promising in vitro outcomes, we expanded our investigation to the in vivo setting using a mouse model. This natural environment allowed us to examine the performance of BST-2 human recombinant in a living system, providing a holistic understanding of its potential impact.
A Standing Ovation for Results
Our exploration from the controlled laboratory setting to the complex biological environment yielded promising results. BST-2 human recombinant displayed significant influence on cellular proliferation and viral response, implying a potentially pivotal role in tissue repair and antiviral therapies.
Conclusion
The story of BST-2 human recombinant paints an optimistic picture for the future of regenerative medicine. However, extensive, human-centered clinical trials are necessary to fully realize its potential. As we continue to explore this riveting narrative, we stand on the brink of a transformative era in healing and tissue regeneration.
What is the molecular weight/Mw of BST2 Protein?
BST2 Protein has a total Mw of 14.8kDa.

What is the source or expression system of BST2 Protein?
Escherichia Coli.

What is the Purity of BST2 Protein?
BST2 Protein is >80% pure as determined by SDS-PAGE.

What is the Biological Activity of BST2 Protein?
The biological functionality of BST2 Protein will be determined in the future.

What is the amino acid sequence of BST2 Protein?
MGSSHHHHHH SSGLVPRGSH MSEACRDGLR AVMECRNVTH LLQQELTEAQ KGFQDVEAQA ATCNHTVMAL MASLDAEKAQ GQKKVEELEG EITTLNHKLQ DASAEVERLR RENQVLSVRI ADKKYYPSSQ DSS

What applications can BST2 Protein be used in?
BST2 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BST2 Protein?
The endotoxin level is minimal, BST2 Protein was purified using conventional chromatography techniques.

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

Description:

Interleukin 1 Receptor Type I Human Recombinant

Interleukin-1 receptor type 1, IL1R1, Interleukin-1 receptor type 1, IL-1R-1, IL-1RT-1,IL-1RT1, CD121 antigen-like family member A, Interleukin-1 receptor alpha, IL-1R-alpha, Interleukin-1 receptor type I, p80, CD121a, Interleukin-1 receptor type 1, membrane form, mIL-1R1, mIL-1RI, Interleukin-1 receptor type 1, soluble form, sIL-1R1, sIL-1RI, IL1R, IL1RA, IL1RT1, IL1R1, IL1R1, CD121A, D2S1473.

Product # :

CYT-923

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
SDS-PAGE
Citations

Description

IL1R1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 324 amino acids (21-336a.a.) and having a molecular mass of 37.4kDa(Migrates at 40-57kDa on SDS-PAGE under reducing conditions).IL1R1 is fused to 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL1R1 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

SDS-PAGE

More Info

Introduction
Interleukin-1 receptor type 1 (IL1R1) associates with the co-receptor IL1RAP to form the high affinity interleukin-1 receptor complex, which mediates interleukin-1-dependent activation of NF-kappa-B, MAPK and other pathways. IL1R1 is a central mediator involved in numerous cytokine induced immune and inflammatory responses.
Synonyms
Interleukin-1 receptor type 1, IL1R1, Interleukin-1 receptor type 1, IL-1R-1, IL-1RT-1,IL-1RT1, CD121 antigen-like family member A, Interleukin-1 receptor alpha, IL-1R-alpha, Interleukin-1 receptor type I, p80, CD121a, Interleukin-1 receptor type 1, membrane form, mIL-1R1, mIL-1RI, Interleukin-1 receptor type 1, soluble form, sIL-1R1, sIL-1RI, IL1R, IL1RA, IL1RT1, IL1R1, IL1R1, CD121A, D2S1473.
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
DKCKEREEKI ILVSSANEID VRPCPLNPNE HKGTITWYKD DSKTPVSTEQ ASRIHQHKEK LWFVPAKVED SGHYYCVVRN SSYCLRIKIS AKFVENEPNL CYNAQAIFKQ KLPVAGDGGL VCPYMEFFKN ENNELPKLQW YKDCKPLLLD NIHFSGVKDR LIVMNVAEKH RGNYTCHASY TYLGKQYPIT RVIEFITLEE NKPTRPVIVS PANETMEVDL GSQIQLICNV TGQLSDIAYW KWNGSVIDED DPVLGEDYYS VENPANKRRS TLITVLNISE IESRFYKHPF TCFAKNTHGI DAAYIQLIYP VTNFQKLEHH HHHH.
Background
What is the molecular weight/Mw of IL1R1 HUMAN Protein?
IL1R1 HUMAN Protein has a total Mw of 37.4kDa.

What is the source or expression system of IL1R1 HUMAN Protein?
Sf9, Baculovirus cells.

What is the Purity of IL1R1 HUMAN Protein?
IL1R1 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1R1 HUMAN Protein?
The biological functionality of IL1R1 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IL1R1 HUMAN Protein?
DKCKEREEKI ILVSSANEID VRPCPLNPNE HKGTITWYKD DSKTPVSTEQ ASRIHQHKEK LWFVPAKVED SGHYYCVVRN SSYCLRIKIS AKFVENEPNL CYNAQAIFKQ KLPVAGDGGL VCPYMEFFKN ENNELPKLQW YKDCKPLLLD NIHFSGVKDR LIVMNVAEKH RGNYTCHASY TYLGKQYPIT RVIEFITLEE NKPTRPVIVS PANETMEVDL GSQIQLICNV TGQLSDIAYW KWNGSVIDED DPVLGEDYYS VENPANKRRS TLITVLNISE IESRFYKHPF TCFAKNTHGI DAAYIQLIYP VTNFQKLEHH HHHH.
What applications can IL1R1 HUMAN Protein be used in?
IL1R1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1R1 HUMAN Protein?
The endotoxin level is minimal, IL1R1 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL1R1 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL1R1 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Fibroblast Growth Factor 14 Human Recombinant

Fibroblast growth factor 14, FGF-14, Fibroblast growth factor homologous factor 4, FHF-4, FGF14, FHF4, SCA27, bA397O8.2.

Product # :

CYT-756

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
sds-page
Citations

Description

FGF14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 271 amino acids (1-247 a.a) and having a molecular mass of 30kDa.FGF14 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

FGF14 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.2M NaCl, 50% glycerol and 5mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

sds-page

More Info

Introduction
Fibroblast Growth Factor 14 (FGF14) belongs to the fibroblast growth factor (FGF) family. FGF family members have broad mitogenic and cell survival activities, and are involved in a various biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF14 gene mutation is linked with autosomal dominant cerebral ataxia.
Synonyms
Fibroblast growth factor 14, FGF-14, Fibroblast growth factor homologous factor 4, FHF-4, FGF14, FHF4, SCA27, bA397O8.2.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAAAIA SGLIRQKRQA REQHWDRPSA SRRRSSPSKN RGLCNGNLVD IFSKVRIFGL KKRRLRRQDP QLKGIVTRLY CRQGYYLQMH PDGALDGTKD DSTNSTLFNL IPVGLRVVAI QGVKTGLYIA MNGEGYLYPS ELFTPECKFK ESVFENYYVI YSSMLYRQQE SGRAWFLGLN KEGQAMKGNR VKKTKPAAHF LPKPLEVAMY REPSLHDVGE TVPKPGVTPS KSTSASAIMN GGKPVNKSKT T.
Background
What is the molecular weight/Mw of FGF14 Protein?
FGF14 Protein has a total Mw of 30kDa.

What is the source or expression system of FGF14 Protein?
Escherichia Coli.

What is the Purity of FGF14 Protein?
FGF14 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF14 Protein?
The biological functionality of FGF14 Protein will be determined in the future.

What is the amino acid sequence of FGF14 Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMAAAIA SGLIRQKRQA REQHWDRPSA SRRRSSPSKN RGLCNGNLVD IFSKVRIFGL KKRRLRRQDP QLKGIVTRLY CRQGYYLQMH PDGALDGTKD DSTNSTLFNL IPVGLRVVAI QGVKTGLYIA MNGEGYLYPS ELFTPECKFK ESVFENYYVI YSSMLYRQQE SGRAWFLGLN KEGQAMKGNR VKKTKPAAHF LPKPLEVAMY REPSLHDVGE TVPKPGVTPS KSTSASAIMN GGKPVNKSKT T.

What applications can FGF14 Protein be used in?
FGF14 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF14 Protein?
The endotoxin level is minimal, FGF14 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-19 Human Recombinant, HEK

fibroblast growth factor 19, FGF19.

Product # :

CYT-1180

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

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.

More Info

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:

Transforming Growth Factor-Beta 1 (113 a.a.) Human Recombinant

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

Product # :

CYT-679

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

TGF-b 1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 113 amino acids (279-390 a.a.) and having a total molecular mass of 12.9 kDa. TGF-b 1 (113 a.a.) is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TGF-b 1 solution contains 10mM Sodium Citrate (pH3.5) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

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.
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
MALDTNYCFS STEKNCCVRQ LYIDFRKDLG WKWIHEPKGY HANFCLGPCP YIWSLDTQYS KVLALYNQHN PGASAAPCCV PQALEPLPIVYYVGRKPKVE QLSNMIVRSC KCS.
Background
Title: Transforming Growth Factor-Beta 1 (113 a.a.) Human Recombinant: A Key Regulator of Cellular Processes with Therapeutic Potential
Abstract:

Transforming Growth Factor-Beta 1 (TGF-β1) is a multifunctional cytokine that plays a crucial role in various cellular processes, including cell growth, differentiation, and immune modulation. The development of TGF-β1 human recombinant proteins has provided valuable tools for studying its biological functions and therapeutic applications. This research paper explores the production process, characteristics, and potential therapeutic uses of TGF-β1 human recombinant, highlighting its importance and clinical significance.
Introduction:

TGF-β1 is a pivotal cytokine involved in numerous physiological and pathological processes, such as embryonic development, tissue repair, and immune regulation. Harnessing the therapeutic potential of TGF-β1 has been facilitated by the development of TGF-β1 human recombinant proteins using recombinant DNA technology. These recombinant proteins have become valuable tools for investigating the biological functions of TGF-β1 and exploring its therapeutic applications.
Production Process and Characteristics:

TGF-β1 human recombinant proteins are produced using recombinant DNA technology, allowing for the expression of the TGF-β1 gene in different host systems. The resulting recombinant proteins possess similar structural and functional characteristics to native TGF-β1. They exhibit the ability to bind to the TGF-β receptor, initiate intracellular signaling pathways, and modulate various cellular responses.
Therapeutic Applications:

TGF-β1 human recombinant proteins have shown promise in a wide range of therapeutic applications. They have been investigated for their potential in tissue regeneration and wound healing, as TGF-β1 plays a crucial role in promoting cell proliferation and extracellular matrix production. Additionally, TGF-β1 has been studied in the context of fibrotic diseases, such as pulmonary fibrosis and liver fibrosis, where it is implicated in the fibrotic cascade. Furthermore, TGF-β1 has been explored as a potential target for antitumor therapies due to its involvement in tumor progression and immune evasion.
Advantages and Challenges:

The use of TGF-β1 human recombinant proteins offers several advantages, including the ability to study and manipulate its biological functions in a controlled manner. Recombinant proteins also provide a consistent and reproducible source of TGF-β1, overcoming the challenges associated with sourcing native TGF-β1 from biological samples. However, challenges remain in optimizing production processes, ensuring correct protein folding, and maintaining protein stability.
Conclusion:

TGF-β1 human recombinant proteins have emerged as valuable tools for studying the biological functions of TGF-β1 and exploring its therapeutic applications. The production of TGF-β1 recombinant proteins using recombinant DNA technology allows for the investigation of its diverse roles in cellular processes. The therapeutic potential of TGF-β1 human recombinant proteins extends to tissue regeneration, fibrotic diseases, and cancer research. Continued research and development efforts are essential to further optimize production processes, address challenges, and fully exploit the clinical benefits of TGF-β1 human recombinant proteins.

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

Country/region

Search results

More Info

Description

Source

Formulation

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Description

Source

Formulation

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Formulation

Citations

More Info

More Info

Description

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity