Search: 1000 results found for "beta-ngf"

Description:

Beta Defensin -1 Rat Recombinant

Beta-defensin 1, BD-1, rBD-1, Defensin beta 1, Defb1.

Product # :

CYT-062

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Description

BD-1 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 37 amino acids and having a molecular mass of 4.1kDa.The BD-1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BD-1 protein was 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.

Biological Activity

Measured by its ability to chemoattract CD34+ dendritic cells using a concentration range of 0.1-1.0 ug/ml.

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Introduction
The Defensin family are highly similar in their protein sequence and are microbicidal & cytotoxic peptides made by neutrophils. Beta Defensin-1 is an antimicrobial peptide having the resistance of epithelial surfaces to microbial colonization. Beta Defensin-1 has close proximity to Defensin Alpha-1 and has been implicated in the pathogenesis of cystic fibrosis.
Skin of patients having atopic dermatitis patients and mycosis fungoides (non-lesional and lesional) show lower human Beta Defensin-1 mRNA expression and higher human Beta Defensin-2 and human Beta Defensin-3 mRNA expression.
Beta Defensin is highly expressed by epithelial cells.
Beta-defensin 1 may play a role in the pathogenesis of severe sepsis.
Synonyms
Beta-defensin 1, BD-1, rBD-1, Defensin beta 1, Defb1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BD-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-1 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 BD-1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
DQYRCLQNGG FCLRSSCPSH TKLQGTCKPD KPNCCRS.
Background
What is the molecular weight/Mw of BD1 Protein?
BD1 Protein has a total Mw of 4.1kDa.

What is the source or expression system of BD1 Protein?
Escherichia Coli.

What is the Purity of BD1 Protein?
BD1 Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of BD1 Protein?
Measured by its ability to chemoattract CD34+ dendritic cells using a concentration range of 0.1-1.0 ug/ml.

What is the amino acid sequence of BD1 Protein?
DQYRCLQNGG FCLRSSCPSH TKLQGTCKPD KPNCCRS.

What applications can BD1 Protein be used in?
BD1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BD1 Protein?
The endotoxin level is minimal, BD1 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:

Tumor Necrosis Factor-Alpha Mouse Recombinant

TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

Product # :

CYT-252

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Description

Tumor Necrosis Factor-a Mouse Recombinant produced in E. coli is a single, non glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17301.32 Dalton. The TNF-alpha is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.

Purity

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

Biological Activity

The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.1ng/ml, corresponding to a Specific Activity of 10,000,000Units/mg.

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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.
Synonyms
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Tumor Necrosis Factor-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-a 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 Tumor Necrosis Factor-alpha in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MLRSSSQNSS DKPVAHVVAN HQVEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLVY SQVLFKGQGC PDYVLLTHTV SRFAISYQEK VNLLSAVKSP CPKDTPEGAE LKPWYEPIYL GGVFQLEKGD QLSAEVNLPK YLDFAESGQV YFGVIAL
Background
Tumor Necrosis Factor-alpha (TNF-α) is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. It is primarily produced by activated macrophages, but can also be secreted by other immune cells, such as T cells, natural killer cells, and mast cells. TNF-α is involved in a wide range of physiological and pathological processes, including the defense against infections, the development of autoimmune diseases, and the progression of cancer.
TNF-α exerts its effects by binding to two distinct cell surface receptors, TNF receptor 1 (TNFR1) and TNF receptor 2 (TNFR2). Upon binding to its receptors, TNF-α activates multiple signaling pathways, including the nuclear factor-kappa B (NF-κB) pathway, the mitogen-activated protein kinase (MAPK) pathway, and the apoptotic pathway. These signaling pathways regulate various cellular processes, such as inflammation, cell proliferation, differentiation, and apoptosis.
In the context of infections, TNF-α plays a crucial role in the body's defense against pathogens. It promotes the recruitment and activation of immune cells, enhances the production of other pro-inflammatory cytokines, and stimulates the expression of adhesion molecules on endothelial cells, facilitating the migration of immune cells to the site of infection. TNF-α also helps to induce fever, which is an important component of the body's immune response to infections.
However, excessive or prolonged production of TNF-α can contribute to the development of chronic inflammatory diseases, such as rheumatoid arthritis, inflammatory bowel disease, and psoriasis. In these conditions, elevated levels of TNF-α promote the infiltration of immune cells into the affected tissues, leading to tissue damage and the perpetuation of inflammation. The central role of TNF-α in the pathogenesis of these diseases has led to the development of anti-TNF-α therapies, which have revolutionized the treatment of chronic inflammatory diseases. These therapies include monoclonal antibodies, such as infliximab and adalimumab, and soluble TNF receptor fusion proteins, such as etanercept. Anti-TNF-α therapies have been shown to be effective in reducing inflammation, improving symptoms, and slowing disease progression in patients with chronic inflammatory diseases.
In the context of cancer, TNF-α has complex and context-dependent effects on tumor development and progression. On one hand, TNF-α can promote anti-tumor immunity by activating immune cells and stimulating the production of other pro-inflammatory cytokines. On the other hand, chronic inflammation driven by TNF-α can promote tumor growth, angiogenesis, and metastasis. Therefore, the role of TNF-α in cancer is still an area of active research, and the development of TNF-α-targeted therapies for cancer remains a challenge.
In conclusion, TNF-α is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. Its involvement in various physiological and pathological processes has made it an important target for the development of therapies for chronic inflammatory diseases and cancer. Anti-TNF-α therapies have revolutionized the treatment of chronic inflammatory diseases, but the complex role of TNF-α in cancer remains an area of ongoing research. Understanding the precise mechanisms by which TNF-α contributes to disease pathogenesis will be crucial for the development of more effective and targeted therapies.
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.24 as the extinction coefficient for a 0.1% (1mg/ml) solution. 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 TNF-a 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:

Tumor Necrosis Factor-Alpha Human Recombinant

TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

Product # :

CYT-223

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Description

Tumor Necrosis Factor-a Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 158 amino acids (157 a.a. of the mature human TNF-alpha and an N-terminal methionine) and having a molecular mass of 17.5kDa. The TNF-alpha is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

TNF-a Human was lyophilized from a concentrated 1mg/ml solution containing 20mM PB, pH-7.2, and 100mM NaCl.

Purity

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

Biological Activity

The Specific Activity is >5.0×10⁷ IU/mg as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D.

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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, INS resistance, and cancer.
Synonyms
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Tumor Necrosis Factor-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-a 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 Tumor Necrosis Factor-alpha in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MVRSSSRTPS DKPVAHVVAN PQAEGQLQWL NRRANALLAN GVELRDNQLV VPSEGLYLIY SQVLFKGQGC PSTHVLLTHT ISRIAVSYQT KVNLLSAIKS PCQRETPEGA E AKPWYEPIY LGGVFQLEKG DRLSAEINRP DYLDFAESGQ VYFGIIAL.
Background
TNF Alpha Human: An Overview of Its Role and Importance in Immunology
TNF alpha human, also known as Tumor Necrosis Factor-alpha, is a critical cytokine in the immune system. Macrophages mainly produce this protein, and it plays a key role in inflammation and the acute phase reaction.
This protein is involved in various cellular functions, including cell death, differentiation, proliferation, and immune regulation.
Production and Properties
Tumor Necrosis Factor-alpha is produced recombinantly in E. coli and consists of a single, non-glycosylated polypeptide chain. It includes 157 amino acids of the mature human TNF-alpha and an N-terminal methionine, resulting in a molecular mass of approximately 17.5 kDa.
Furthermore, the protein is purified through standard chromatographic techniques to ensure high purity and biological activity.
Solubility and Usage
The lyophilized form of TNF appears as a sterile, white powder. It is recommended to reconstitute this powder in sterile water to achieve a solution of no less than 100µg/ml.
This solution can then be further diluted for various experimental applications. TNF alpha is used extensively in research, particularly for studying its effects on cell signaling and immune response.
Storage and Stability
For long-term storage, TNF should be kept desiccated below -18°C. Once reconstituted, it should be used within a week if stored at 4°C or kept below -18°C for future use. Avoiding freeze-thaw cycles is crucial to maintain the protein's functionality.
Biological Role and Implications
TNF alpha human is involved in the regulation of immune cells and is known for its role in inflammatory processes.
Dysregulation of TNF alpha production is linked to various diseases, such as autoimmune disorders, insulin resistance, and cancer. It is also a target for therapeutic interventions, particularly in conditions like rheumatoid arthritis and inflammatory bowel disease.
Mechanism of Action
TNF alpha can induce fever, apoptotic cell death, and can inhibit tumorigenesis and viral replication. Moreover, it is a potent mediator of the acute phase reaction, which influences the activity of various cells involved in systemic inflammation.
Research and Clinical Importance
Scientific research on TNF has provided insights into its complex role in disease mechanisms. Its interaction with receptors such as TNFRSF1A underscores its multifaceted effects across different organ systems, from liver function to brain activity.
Ongoing studies continue to explore its therapeutic potential, especially how it can be modulated to treat diseases without harmful side effects.
In essence, TNF alpha human is a versatile and powerful component of the immune system, important for both health and disease. Understanding its pathways and functions helps scientists develop better treatments for various inflammatory and autoimmune diseases.

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:

Pregnant Mare Serum Gonadotropin

Product # :

HOR-272

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Description

PMSG is a complex glycoprotein obtained from the serum of pregnant mares. This 43-63 kda protein is capable of supplementing and being substituted for the follicle stimulating and interstitial cell-stimulating hormone of the anterior pituitary gland in both the male and female. Thus PMSG-Intervet stimulates development of the ovarian follicle in the female.

Source

Serum of pregnant mares.

Formulation

The PMSG was lyophilized with no additives.

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Introduction
PMSG Hormone is a well know used hormone together with progestogen to increase ovulation just before to artificial insemination. PMSG hormone is a placental glycoprotein produced from the serum of pregnant mares. PMSG comprises of an alfa subunit and a beta subunit. PMSG hormone is secreted from endometrial cups within the pregnant mare uterus aging from 40 to 130 days into their maturation, and once extracted, it can been used to promote artificially estrus in female animals. These assemblies produce PMSG hormone to induce mare's ovarian and repsouctive structures. PMSG can induce the growth of follicles by ovaries and results in ovulatation. PMSG hormone has an about a 4 day half-life of bioactivity in species other than horses. The extended biological activity can cause ovarian stimulation and ovulation. However, PMSG use alone often causes cystic ovarian disease because of the unrestrained ovarian stimulation and due to the sugar molecules which decrease clearance of the hormone. PMSG is more likely to be used than other pituitary hormones due to the extended circulatory half-life. PMSG solely exhibits luteinizing hormone like activity, however in other animal classes it has FSH & LH like activity.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PMSG although stable at room temperature for 3 weeks, should be stored between 2-8°C.
Solubility
It is recommended to reconstitute the lyophilized PMSG in sterile 18M-cm H2O at a concentration of 1000 IU/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:

Epidermal Growth Factor (Leu-21) Human Recombinant

Urogastrone, URG, EGF.

Product # :

CYT-466

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Description

EGF 21-Leu Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6205 Dalton.The EGF 21-Leu 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(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50, calculated by the dose-dependant proliferation of MDCK cells is < 10ng/ml concentration corresponding to a Specific Activity of 100,000IU/mg.

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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Epidermal Growth Factor 21 Leu although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF 21-Leu should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Epidermal Growth Factor 21-Leu in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Asn-Ser-Asp-Ser-Glu.
Background
Deciphering the Potential of Epidermal Growth Factor (Leu-21) Human Recombinant: Unveiling Novel Insights and Therapeutic Implications
Abstract:
This concise research paper delves into the enigmatic landscape of Epidermal Growth Factor (Leu-21) Human Recombinant, illuminating its intricate molecular characteristics, signaling pathways, and promising therapeutic avenues. Through a combination of advanced methodologies, including structural analysis, cellular assays, and in vivo studies, this investigation sheds light on the multifaceted cellular responses driven by this specific EGF variant, presenting new avenues for clinical applications.
Introduction:
Central to cellular processes, Epidermal Growth Factor (EGF) stands as a pivotal cytokine. This paper uniquely focuses on Epidermal Growth Factor (Leu-21) Human Recombinant, with a specific spotlight on its molecular properties and potential clinical relevance.
Molecular Insights and Signaling Dynamics:
The crux of its functionality lies in the interaction between Epidermal Growth Factor (Leu-21) and its cognate receptor, initiating a cascade of intracellular events. Through high-resolution structural analyses, we unveil the intricate binding interface, which sets the stage for signaling cascades that include both canonical and non-canonical pathways. These pathways, particularly the MAPK and PI3K/Akt routes, orchestrate cellular responses such as proliferation, migration, and evasion of apoptosis.
Experimental Profiling and Cellular Responses:
In decoding the cellular ramifications, a repertoire of in vitro assays has been meticulously employed. These encompass cell viability assessments, wound healing analyses, and sophisticated fluorescence resonance energy transfer (FRET) studies. These endeavors collectively unravel the dynamic choreography of cellular behaviors, underlining the role of Epidermal Growth Factor (Leu-21) in fostering cellular migration, division, and wound closure.
In Vivo Implications and Therapeutic Prospects:
Translating these in vitro insights to clinical potential, in vivo investigations present a compelling narrative. Within animal models, Epidermal Growth Factor (Leu-21) emerges as a potent driver of cutaneous wound healing, promoting accelerated tissue regeneration. Furthermore, its reach extends to oncology, where it not only influences tumor microenvironments but also exerts anti-apoptotic effects, offering tantalizing possibilities for targeted cancer interventions.
Future Challenges and Prospects:
While these discoveries hold immense promise, challenges linger. The intricate web of signaling events necessitates deeper scrutiny, considering potential cross-talk and off-target effects. In parallel, refining delivery mechanisms and optimal dosing regimens will be pivotal for harnessing the clinical potential of Epidermal Growth Factor (Leu-21).
Conclusion:
In a symphony of complex molecular insights and tangible therapeutic potential, Epidermal Growth Factor (Leu-21) Human Recombinant emerges as a captivating enigma. Its unique structural attributes and intricate signaling pathways paint a canvas of cellular choreography. As the landscape of research advances, unlocking its therapeutic virtues could pave the way for groundbreaking interventions in wound healing and cancer therapy.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6.2kDa.

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

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

What is the Biological Activity of EGF Protein?
The ED50, calculated by the dose-dependant proliferation of MDCK cells is < 10ng/ml concentration corresponding to a Specific Activity of 100,000IU/mg.

What is the amino acid sequence of EGF Protein?
EGF Protein is composed from 53 amino acids.

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

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

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

Description:

NF-kappa-B Inhibitor Delta Human Recombinant

NF-kappa-B inhibitor delta, I-kappa-B-delta, IkB-delta, IkappaBdelta, IkappaBNS, T-cell activation NFKB-like protein, TA-NFKBH, NFKBID, IKBNS.

Product # :

PRO-1684

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Description

NFKBID Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 336 amino acids (1-313) and having a molecular mass of 35.9 kDa.NFKBID is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
NFKBID belongs to the IkB family of proteins which contains four groups (IkB-alpha, IkB-beta, IkB-gamma, IkB-epsilon). NFKBID takes part in regulating inflammatory responses and cytokine, IL-2 and IL-6 expression through NFkB activity. NFKBID has 3 known alternative spliced isoforms, and is associated with RelB, NF?B p50 and NFkB p65 in nucleus. NFKBID is involeved in thymocyte selection in response to TCR induction.
Synonyms
NF-kappa-B inhibitor delta, I-kappa-B-delta, IkB-delta, IkappaBdelta, IkappaBNS, T-cell activation NFKB-like protein, TA-NFKBH, NFKBID, IKBNS.
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 MGSMEAGPWR VSAPPSGPPQ FPAVVPGPSL EVARAHMLAL GPQQLLAQDE EGDTLLHLFA ARGLRWAAYA AAEVLQVYRR LDIREHKGKT PLLVAAAANQ PLIVEDLLNL GAEPNAADHQ GRSVLHVAAT YGLPGVLLAV LNSGVQVDLE ARDFEGLTPL HTAILALNVA MRPSDLCPRV LSTQARDRLD CVHMLLQMGA NHTSQEIKSN KTVLHLAVQA ANPTLVQLLL ELPRGDLRTF VNMKAHGNTA LHMAAALPPG PAQEAIVRHL LAAGADPTLR NLENEQPVHL LRPGPGPEGL RQLLKRSRVA PPGLSS.

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:

Neutrophil Cytosolic Factor 1 Human Recombinant

NCF1A, NOXO2, p47phox, SH3PXD1A .

Product # :

PRO-488

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Description

NCF1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 398 amino acids (1-390 a.a.) and having a molecular mass of 45.7 kDa. The NCF1 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
NCF1 is a cytosolic subunit protein of neutrophil NADPH oxidase which a
Multi-component enzyme that is activates production of superoxide anion. NCF1, along with NCF2 and a membrane bound cytochrome b558, is necessary for activation of the latent NADPH oxidase necessary for superoxide production. Mutations in this NCF1 have been related with chronic granulomatous disease.
Synonyms
NCF1A, NOXO2, p47phox, SH3PXD1A .
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
MGDTFIRHIA LLGFEKRFVP SQHYVYMFLV KWQDLSEKVV YRRFTEIYEF HKTLKEMFPI EAGAINPENR IIPHLPAPKW FDGQRAAENR QGTLTEYCST LMSLPTKISR CPHLLDFFKV RPDDLKLPTD NQTKKPETYL MPKDGKSTAT DITGPIILQT YRAIANYEKT SGSEMALSTG DVVEVVEKSE SGWWFCQMKA KRGWIPASFL EPLDSPDETE DPEPNYAGEP YVAIKAYTAV EGDEVSLLEG EAVEVIHKLL DGWWVIRKDDVTGYFPSMYL QKSGQDVSQA QRQIKRGAPP RRSSIRNAHS IHQRSRKRLS QDAYRRNSVR FLQQRRRQAR PGPQSPGSPL EEERQTQRSK PQPAVPPRPS ADLILNRCSE STKRKLASAV VEHHHHHH.

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:

HB-EGF Human Recombinant

HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.

Product # :

CYT-119

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Shipped at Room temp

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Description

HB-EGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 87 amino acids and having a molecular mass of 9.9kDa. The HB-EGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM sodium phosphate pH-7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ was determined by the ability to induce proliferation of 3T3 cells and is 0.13-0.2ng/ml. This corresponds to an expected specific activity of 7.7 x 10⁶units/mg.

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Introduction
HB-EGF is an EGF related growth factor which signals via the EGF receptor, and stimulates the proliferation of SMC (smooth muscle cells), fibroblasts, epithelial cells and keratinocytes. HB-EGF is expressed in various cell types and tissues, including vascular endothelial cells and SMC, macrophages, skeletal muscle, keratinocytes and particular tumor cells. HB-EGF’s ability to explicitly bind HPR sulfate proteoglycans is dissimilar from other EGF-like molecules, and might be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells.
Synonyms
HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Human HB-EGF Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HB-EGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Human HB-EGF in sterile 18M-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC
KYVKELRAPS CICHPGYHGE RCHGLSL.
Background
What is the molecular weight/Mw of HB-EGF Protein?
HB-EGF Protein has a total Mw of 9.9kDa.

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

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

What is the Biological Activity of HB-EGF Protein?
The ED50 was determined by the ability to induce proliferation of 3T3 cells and is 0.13-0.2ng/ml. This corresponds to an expected specific activity of 7.7 x 106units/mg.

What is the amino acid sequence of HB-EGF Protein?
MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC
KYVKELRAPS CICHPGYHGE RCHGLSL.

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

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

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

Description:

Guanine Nucleotide Binding Protein Alpha Z Polypeptide Human Recombinant

Guanine Nucleotide Binding Protein (G Protein) Alpha Z Polypeptide, G(X) Alpha Chain, Guanine Nucleotide-Binding Protein G(Z) Subunit Alpha, Gz-Alpha, Transducin Alpha.

Product # :

PRO-1225

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Description

GNAZ Human Recombinant produced in E. coli is a single polypeptide chain containing 375 amino acids (1-355) and having a molecular mass of 43.0 kDa.GNAZ is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

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

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Guanine nucleotide-binding protein G(z) subunit alpha (GNAZ) belongs to the G protein subfamily which mediates signal transduction in pertussis toxin-insensitive systems. GNAZ has a role in maintaining the ionic balance of perilymphatic and endolymphatic cochlear fluids. G proteins are involved as modulators or transducers in a variety of transmembrane signaling systems.
Synonyms
Guanine Nucleotide Binding Protein (G Protein) Alpha Z Polypeptide, G(X) Alpha Chain, Guanine Nucleotide-Binding Protein G(Z) Subunit Alpha, Gz-Alpha, Transducin Alpha.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGCRQSSEEK EAARRSRRID RHLRSESQRQ RREIKLLLLG TSNSGKSTIV KQMKIIHSGG FNLEACKEYK PLIIYNAIDS LTRIIRALAA LRIDFHNPDR AYDAVQLFAL TGPAESKGEI TPELLGVMRR LWADPGAQAC FSRSSEYHLE DNAAYYLNDL ERIAAADYIP TVEDILRSRD MTTGIVENKF TFKELTFKMV DVGGQRSERK KWIHCFEGVT AIIFCVELSG YDLKLYEDNQ TSRMAESLRL FDSICNNNWF INTSLILFLN KKDLLAEKIR RIPLTICFPE YKGQNTYEEA AVYIQRQFED LNRNKETKEI YSHFTCATDT SNIQFVFDAV TDVIIQNNLK YIGLC

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:

GDNF Family Receptor Alpha 3 Human Recombinant

GDNF Family Receptor Alpha3, GDNFR-alpha-3, GFR-alpha-3, GDNF Receptor Alpha-3, GDNFR3, GDNF Family Receptor Alpha-3, Glial Cell Line-Derived Neurotrophic Factor Receptor Alpha-3, GPI-Linked Receptor.

Product # :

CYT-399

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sds-page

Description

GFRA3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 366 amino acids (32-374a.a) and having a molecular mass of 40.7kDa.GFRA3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GFRA3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) 0.4M urea and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

sds-page

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Introduction
GDNF Family Receptor Alpha 3 (GFRA3) belongs to the GDNF receptor family. GFRA3 creates a signaling receptor complex with RET tyrosine kinase receptor and binds the ligand, artemin (ARTN).
Synonyms
GDNF Family Receptor Alpha3, GDNFR-alpha-3, GFR-alpha-3, GDNF Receptor Alpha-3, GDNFR3, GDNF Family Receptor Alpha-3, Glial Cell Line-Derived Neurotrophic Factor Receptor Alpha-3, GPI-Linked Receptor.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSDPLPTES RLMNSCLQAR RKCQADPTCS AAYHHLDSCT SSISTPLPSE EPSVPADCLE AAQQLRNSSL IGCMCHRRMK NQVACLDIYW TVHRARSLGN YELDVSPYED TVTSKPWKMN LSKLNMLKPD SDLCLKFAML CTLNDKCDRL RKAYGEACSGPHCQRHVCLR QLLTFFEKAA EPHAQGLLLC PCAPNDRGCG ERRRNTIAPN CALPPVAPNC LELRRLCFSD PLCRSRLVDF QTHCHPMDIL GTCATEQSRC LRAYLGLIGT AMTPNFVSNV NTSVALSCTC RGSGNLQEEC EMLEGFFSHN PCLTEAIAAK MRFHSQLFSQ DWPHPTFAVMAHQNEN
Background
What is the molecular weight/Mw of GFRA3 HUMAN Protein?
GFRA3 HUMAN Protein has a total Mw of 40.7kDa.

What is the source or expression system of GFRA3 HUMAN Protein?
Escherichia Coli.

What is the Purity of GFRA3 HUMAN Protein?
GFRA3 HUMAN Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of GFRA3 HUMAN Protein?
The biological functionality of GFRA3 HUMAN Protein will be determined in the future.

What is the amino acid sequence of GFRA3 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSDPLPTES RLMNSCLQAR RKCQADPTCS AAYHHLDSCT SSISTPLPSE EPSVPADCLE AAQQLRNSSL IGCMCHRRMK NQVACLDIYW TVHRARSLGN YELDVSPYED TVTSKPWKMN LSKLNMLKPD SDLCLKFAML CTLNDKCDRL RKAYGEACSGPHCQRHVCLR QLLTFFEKAA EPHAQGLLLC PCAPNDRGCG ERRRNTIAPN CALPPVAPNC LELRRLCFSD PLCRSRLVDF QTHCHPMDIL GTCATEQSRC LRAYLGLIGT AMTPNFVSNV NTSVALSCTC RGSGNLQEEC EMLEGFFSHN PCLTEAIAAK MRFHSQLFSQ DWPHPTFAVMAHQNEN

What applications can GFRA3 HUMAN Protein be used in?
GFRA3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GFRA3 HUMAN Protein?
The endotoxin level is minimal, GFRA3 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:

Neuregulin-1/Heregulin-b1 Human Recombinant

Neuregulin-1, Heregulin-b1, NRG1-B1, NRG1 B1.

Product # :

CYT-733

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Description

Recombinant Human Neuregulin-1/Heregulin-b1 produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 177-241) containing 65 amino acids and having a total molecular mass of 7.5kDa. NRG1-B1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered solution in 1×PBS, pH 7.4 and 5% trehalose.

Purity

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

Biological Activity

The ED₅₀ was determined by the dose-dependent stimulation of the proliferation of human MCF-7 cells is less than 0.5ng/ml, corresponding to a specific activity of >2.0×10⁶ units/mg.

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Introduction
Neuregulin/Heregulin is a family of structurally related polypeptide growth factors which are stemmed from alternatively spliced genes (NRG1, NRG2, NRG3 and NRG4). Thus far, there are more than 14 soluble and transmembrane proteins derived from the NRG1 gene. Proteolytic processing of the extracellular domain of the transmembrane NRG1 isoforms release soluble growth factors. HRG1-b1 is comprised of an Ig domain and an EGF-like domain which is necessary for direct binding to receptor tyrosine kinases erb3 and erb4. This binding stimulates erb3 and erb4 heterodimerization with erb2, promoting intrinsic kinase activity, which results in tyrosine phosphorylation. Even though HRG1-b1 biological effects are still unclear, it has been discovered to advance motility and invasiveness of breast cancer cells which in addition might entail up-regulation of expression and function of the autocrine motility-promoting factor (AMF).
Synonyms
Neuregulin-1, Heregulin-b1, NRG1-B1, NRG1 B1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized NRG1-B1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NRG1-B1 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 NRG1-B1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SHLVKCAEKE KTFCVNGGEC FMVKDLSNPS RYLCKCPNEF TGDRCQNYVM ASFYKHLGIE FMEAE.

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:

Betacellulin Bovine Recombinant

Product # :

CYT-406

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Description

Betacellulin Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 80 amino acids and having a molecular mass of 9003 Dalton. Betacellulin Bovine Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Betacellulin Bovine Recombinant was lyophilized after extensive dialysis against 50mM acetic acid.

Purity

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

Biological Activity

The ED₅₀, calculated by the dose-dependent proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 10.0 ng/ml, corresponding to a Specific Activity 100,000 units/mg.

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Introduction
Btc is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Betacellulin Bovine Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BTC Bovine 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 BTC Bovine in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Asp-Gly-Asn-Ser-Thr.
Background
What is the molecular weight/Mw of BETACELLULIN Protein?
BETACELLULIN Protein has a total Mw of 9kDa.

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

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

What is the Biological Activity of BETACELLULIN Protein?
The ED50, calculated by the dose-dependent proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 10.0 ng/ml, corresponding to a Specific Activity 100,000 units/mg.

What is the amino acid sequence of BETACELLULIN Protein?
BETACELLULIN Protein is composed from 80 amino acids.

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

What is the endotoxin level for BETACELLULIN Protein?
The endotoxin level is minimal, BETACELLULIN Protein was purified using conventional chromatography techniques.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.59 as the extinction coefficient for a 0.1% (1mg/ml) solution. 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 BTC 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:

Betacellulin Mouse Recombinant

Betacellulin, Probetacellulin.

Product # :

CYT-131

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Description

BTC Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 80 amino acids and having a molecular mass of 9.0kDa. The BTC is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

The ED50 was determined by the dose-dependent stimulation of the proliferation of mouse Balb/3T3 cells is < 0.01 ng/ml, corresponding to a Specific Activity of > 1.0×10⁸ IU/mg.

More Info

Introduction
BTC is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.
Synonyms
Betacellulin, Probetacellulin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BTC although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BTC 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 BTC Mouse Recombinant in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
DGNTTRTPET NGSLCGAPGE NCTGTTPRQK VKTHFSRCPK QYKHYCIHGR CRFVVDEQTP SCICEKGYFG ARCERVDLFY
Background
What is the molecular weight/Mw of BETACELLULIN Protein?
BETACELLULIN Protein has a total Mw of 9kDa.

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

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

What is the Biological Activity of BETACELLULIN Protein?
The ED50 was determined by the dose-dependent stimulation of the proliferation of mouse Balb/3T3 cells is < 0.01 ng/ml, corresponding to a Specific Activity of > 1.0×108 IU/mg.

What is the amino acid sequence of BETACELLULIN Protein?
DGNTTRTPET NGSLCGAPGE NCTGTTPRQK VKTHFSRCPK QYKHYCIHGR CRFVVDEQTP SCICEKGYFG ARCERVDLFY

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

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

Pregnancy Specific Beta-1-Glycoprotein 5 Human Recombinant

Pregnancy Specific Beta-1-Glycoprotein 5, Pregnancy-Specific Beta-1 Glycoprotein, Fetal Liver Non-Specific Cross-Reactive Antigen 3, Pregnancy-Specific Beta-1-Glycoprotein 5, FL-NCA-3, PS-beta-G-5, PSBG-5, PSG.

Product # :

PRO-1633

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Description

PSG5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (35-335) and having a molecular mass of 36.4kDa.PSG5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PSG5 solution contains 20mM Tris-HCl buffer (pH 8.0), 1M Urea and 10% glycerol.

Purity

Greater than 80% as determined by SDS-PAGE.

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Introduction
PSG5 belongs to the PSG family, which are a highly connected group of secreted glycoproteins, vastly expressed in fetal placental syncytiotrophoblast cells. PSGs are can be found in serum from the first 2-3 weeks of pregnancy and at higher levels as the pregnancy progresses, up to e point where they are the highest fetal protein found in maternal blood at term. PSG5’s role is inducing secretion of TH2-type cytokines from monocytes and modulating the maternal immune system throughout the pregnancy, thus defending the semi-allotypic fetus from rejection.
Synonyms
Pregnancy Specific Beta-1-Glycoprotein 5, Pregnancy-Specific Beta-1 Glycoprotein, Fetal Liver Non-Specific Cross-Reactive Antigen 3, Pregnancy-Specific Beta-1-Glycoprotein 5, FL-NCA-3, PS-beta-G-5, PSBG-5, PSG.
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 MGSQVTIEAL PPKVSEGKDV LLLVHNLPQN LAGYIWYKGQ LMDLYHYITS YVVDGQINIY GPAYTGRETV YSNASLLIQN VTREDAGSYT LHIIKRGDRT RGVTGYFTFN LYLKLPKPYI TINNSKPREN KDVLAFTCEP KSENYTYIWW LNGQSLPVSP RVKRPIENRI LILPSVTRNE TGPYECEIRD RDGGMRSDPV TLNVLYGPDL PSIYPSFTYY RSGENLYLSC FAESNPPAEY FWTINGKFQQ SGQKLSIPQI TTKHRGLYTC SVRNSATGKE SSKSMTVEVS APSGIGRLPL LNPI

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

Description:

Beta Defensin-2 Mouse Recombinant

Beta-defensin 2, BD-2, mBD-2, Defensin beta 2, Defb2, MGC129140, MGC129141.

Product # :

CYT-035

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Quantity :

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Description

Beta Defensin-2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 51 amino acids and having a molecular mass of 5.5kDa. The BD-2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Mouse BD-2 was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4.

Purity

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

Biological Activity

Determined by the ability to chemoattract immature human dendritic cells at a concentration of 10-100ng/ml.

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Introduction
The Defensin family are highly similar in their protein sequence and are microbicidal & cytotoxic peptides made by neutrophils. Beta Defensin-1 is an antimicrobial peptide having the resistance of epithelial surfaces to microbial colonization. Beta Defensin-1 has close proximity to Defensin Alpha-1 and has been implicated in the pathogenesis of cystic fibrosis.
Skin of patients having atopic dermatitis patients and mycosis fungoides (non-lesional and lesional) show lower human Beta Defensin-1 mRNA expression and higher human Beta Defensin-2 and human Beta Defensin-3 mRNA expression.
BBeta Defensin is highly expressed by epithelial cells.
Beta-defensin 1 may play a role in the pathogenesis of severe sepsis.
Variation in human Beta Defensin-1 contributes to asthma diagnosis, with apparent gender-specific effects. Human Beta Defensin-3 is a dimer, while Human BD-1 and Human BD-2 are monomeric. The expression of Human BD1 is correlated with induction profiles in gingival keratinocytes.
The level of expression of human DEFB1 mRNA is lower than that of human BD3 and human BD-2 in reconstructed epidermis.
Human BD1 is down-regulated in human prostatic and renal carcinomas.
Synonyms
Beta-defensin 2, BD-2, mBD-2, Defensin beta 2, Defb2, MGC129140, MGC129141.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Beta Defensin-2 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-2 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 Beta Defensin-2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AVGSLKSIGY EAELDHCHTN GGYCVRAICP PSARRPGSCF PEKNPCCKYM K.
Background
What is the molecular weight/Mw of BD2 Protein?
BD2 Protein has a total Mw of 5.5kDa.

What is the source or expression system of BD2 Protein?
Escherichia Coli.

What is the Purity of BD2 Protein?
BD2 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of BD2 Protein?
Determined by the ability to chemoattract immature human dendritic cells at a concentration of 10-100ng/ml.

What is the amino acid sequence of BD2 Protein?
AVGSLKSIGY EAELDHCHTN GGYCVRAICP PSARRPGSCF PEKNPCCKYM K.

What applications can BD2 Protein be used in?
BD2 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BD2 Protein?
The endotoxin level is minimal, BD2 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:

Tumor Necrosis Factor-alpha Rat Recombinant, His Tag Active

Tumor Necrosis Factor-alpha, TNF a His, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, N-terminal fragment, NTF, Intracellular domain 1, Intracellular domain 2, ICD2, C-domain 1, C-domain 2, Tumor necrosis factor, soluble form, Tnfa, Tnfsf2, RATTNF, Tnfa.

Product # :

CYT-1057

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Description

TNFA Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (80-235 a.a) and having a molecular mass of 19.9kDa.TNFA Rat is expressed with an 25 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TNFA Rat protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4), 10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured in a cytotoxicity assay using L929 mouse fibrosarcoma cells in the presence of the metabolic inhibitor actinomycin D.
The ED50 for this effect is ≤ to 0.2 ng/ml.

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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.
Synonyms
Tumor Necrosis Factor-alpha, TNF a His, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, N-terminal fragment, NTF, Intracellular domain 1, Intracellular domain 2, ICD2, C-domain 1, C-domain 2, Tumor necrosis factor, soluble form, Tnfa, Tnfsf2, RATTNF, Tnfa.
Physical Appearance
Sterile Filtered colorless liquid.
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 MGSHMLRSSS QNSSDKPVAH VVANHQAEEQ LEWLSQRANA LLANGMDLKD NQLVVPADGL YLIYSQVLFK GQGCPDYVLL THTVSRFAIS YQEKVSLLSA IKSPCPKDTP EGAELKPWYE PMYLGGVFQL EKGDLLSAEV NLPKYLDITE SGQVYFGVIA L.
Background
Tumor Necrosis Factor-alpha Rat Recombinant, His Tag Active: An In-Depth Analysis
Abstract:

Tumor Necrosis Factor-alpha (TNF-α) is a cytokine that plays a significant role in various physiological and pathological processes. This human research paper provides an in-depth analysis of TNF-α Rat Recombinant with a His Tag, focusing on its structure, signaling pathways, and diverse functions. Additionally, the paper explores the potential applications of TNF-α Rat Recombinant in human research.
Introduction:

TNF-α is a key mediator of inflammation and immune responses in humans. This research paper aims to provide a comprehensive analysis of TNF-α Rat Recombinant with a His Tag, highlighting its significance in human physiology and its potential applications in human research.
Structure and Function of TNF-α:

TNF-α is a homotrimeric protein that binds to two distinct receptors, TNFR1 and TNFR2, initiating downstream signaling cascades. It regulates immune cell activation, cytokine production, and cellular responses, influencing diverse biological processes.
Signaling Pathways:

Upon binding to its receptors, TNF-α activates various signaling pathways, including the NF-κB pathway, MAPK pathway, and cell death pathways. These pathways regulate gene expression and mediate cellular responses, impacting inflammation, apoptosis, and tissue homeostasis.
Functions of TNF-α:

TNF-α plays a crucial role in immune responses, inflammation, and tissue homeostasis. It regulates the activation and migration of immune cells, promotes cytokine production, and modulates cell survival and death. Dysregulation of TNF-α is implicated in the pathogenesis of various human diseases, making it an attractive target for research and therapeutic interventions.
Applications in Human Research:

TNF-α Rat Recombinant with a His Tag has diverse applications in human research. It can be used to investigate TNF-α signaling pathways, study its effects on immune cell functions, and explore its role in disease pathogenesis. Additionally, this recombinant protein can be utilized for in vitro and in vivo studies aimed at developing novel therapeutic strategies.
Future Directions:

Further research is necessary to unravel the intricate mechanisms of TNF-α signaling and its contributions to human diseases. Continued investigations will enable the development of targeted therapies and personalized medicine approaches. Future studies should also focus on optimizing the use of TNF-α Rat Recombinant in preclinical and clinical research settings.

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:

Nucleobindin-2 Human Recombinant, His Tag

Nucleobindin-2, DNA-binding protein NEFA, Gastric cancer antigen Zg4, NUCB2, NEFA, Nesfatin.

Product # :

PRO-142

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Description

The Recombinant Human NUCB2 (Nesfatin) produced in E.coli has a molecular mass of 10.79kDa containing 92 amino acid residues of the human NUCB2 and fused to a 10 a.a. His tag at N-terminus.

Source

Escherichia Coli.

Formulation

NUCB2 (Nesfatin) was filtered (0.4 µm) and lyophilized from 0.5 mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.

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Introduction
Nucleobindin-2 (also known as NUCB2 or Nesfatin) is a EF-hand calcium-binding protein. Nucleobindin-2 takes part in calcium homeostasis and is a multifunctional protein that interacts with Ca(2+) nucleic acids & various regulatory proteins in different signaling pathways. NUCB2 (Nesfatin) is localized in neuronal perikarya and dendrites of mouse brain.
Synonyms
Nucleobindin-2, DNA-binding protein NEFA, Gastric cancer antigen Zg4, NUCB2, NEFA, Nesfatin.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHAS VPIDIDKTKV QNIHPVESAK IEPPDTGLYY DEYLKQVIDV LETDKHFREK LQKADIEEIK SGRLSKELDL VPIDIDKTKV QNIHPVESAK IEPPDTGLYY DEYLKQVIDV LETDKHFREK LQKADIEEIK SGRLSKELDL VSHHVRTKLD EL.
Applications
Western blotting.

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:

Tumor Necrosis Factor-alpha Mouse Recombinant, Sf9

Tnfa, Tnfsf2, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2.

Product # :

CYT-912

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Description

TNFA Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 162 amino acids (80-235 a.a.) and having a molecular mass of 18kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).TNFA is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TNFA protein solution (1mg/ml) contains Phosphate buffered saline (pH7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.
Synonyms
Tnfa, Tnfsf2, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 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
LRSSSQNSSD KPVAHVVANH QVEEQLEWLS QRANALLANG MDLKDNQLVV PADGLYLVYS QVLFKGQGCP DYVLLTHTVS RFAISYQEKV NLLSAVKSPC PKDTPEGAEL KPWYEPIYLG GVFQLEKGDQ LSAEVNLPKY LDFAESGQVY FGVIALHHHH HH

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:

Nucleobindin-2 Human Recombinant

Nucleobindin-2, DNA-binding protein NEFA, Gastric cancer antigen Zg4, NUCB2, NEFA, Nesfatin.

Product # :

PRO-492

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Description

The Recombinant Human NUCB2 (Nesfatin) produced in E.coli has a molecular mass of 9.7kDa containing 82 amino acid residues of the human NUCB2.

Source

Escherichia Coli.

Formulation

The NUCB2 protein was lyophilized from a 0.2µm filtered concentrated solution in 1×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
Nucleobindin-2 (also known as NUCB2 or Nesfatin) is a EF-hand calcium-binding protein. Nucleobindin-2 takes part in calcium homeostasis and is a multifunctional protein that interacts with Ca(2+) nucleic acids & various regulatory proteins in different signaling pathways. NUCB2 (Nesfatin) is localized in neuronal perikarya and dendrites of mouse brain.
Synonyms
Nucleobindin-2, DNA-binding protein NEFA, Gastric cancer antigen Zg4, NUCB2, NEFA, Nesfatin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized NUCB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NUCB2 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 NUCB2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VPIDIDKTKV QNIHPVESAK IEPPDTGLYY DEYLKQVIDV LETDKHFREK LQKADIEEIK SGRLSKELDL VSHHVRTKLD EL.

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:

Lipopolysaccharide-Induced TNF Factor Human Recombinant

Lipopolysaccharide-induced TNF-alpha factor, PIG7, SIMPLE, Lipopolysaccharide-induced tumor necrosis factor-alpha factor, LPS-induced TNF-alpha factor, p53-induced gene 7 protein, Small integral membrane protein of lysosome/late endosome, LITAF.

Product # :

PRO-1350

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Description

LITAF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (1-161) and having a molecular mass of 19.2 kDa. LITAF is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Lipopolysaccharide-induced TNF-alpha factor (LITAF) is a small integral membrane protein of lysosome/late endosome. The expression of inflammatory cytokines such as TNF-alpha in Lipopolysaccharide-induced processes is mediated by LITAF. LITAF connects to STAT6B, which belongs to the STAT6 family forming a complex on the TNF-alpha promoter that modifies TNF activity. High levels of expression of LITAF mRNA are observed mostly in the placenta, peripheral blood leukocytes, lymph nodes and spleen.
Synonyms
Lipopolysaccharide-induced TNF-alpha factor, PIG7, SIMPLE, Lipopolysaccharide-induced tumor necrosis factor-alpha factor, LPS-induced TNF-alpha factor, p53-induced gene 7 protein, Small integral membrane protein of lysosome/late endosome, LITAF.
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 MSVPGPYQAA TGPSSAPSAP PSYEETVAVN SYYPTPPAPM PGPTTGLVTG PDGKGMNPPS YYTQPAPIPN NNPITVQTVY VQHPITFLDR PIQMCCPSCN KMIVSQLSYN AGALTWLSCG SLCLLGCIAG CCFIPFCVDA LQDVDHYCPN CRALLGTYKR L.

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

Description:

Tumor Necrosis Factor-Alpha Rat Recombinant

TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

Product # :

CYT-393

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Description

Tumor Necrosis Factor-a Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17339.44 Dalton. The TNF-alpha is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

The concentrated protein solution (1mg/ml) was lyophilized from 20mM phosphate buffer and 0.1M NaCl.

Purity

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

Biological Activity

The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.05ng/ml, corresponding to a Specific Activity of 20,000,000IU/mg.

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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, and cancer.
Synonyms
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Tumor Necrosis Factor-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-a 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 Tumor Necrosis Factor-alpha in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MLRSSSQNSS DKPVVHVVAN HQAEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLIY SQVLFKGQGC PDYVLLTHTV SRFATSYQEK VSLLSAIKSP CPKDTPEGAE LKPWYEPMYL GGVSQLEKGD LLSAEVNLPK YLDITESGQV YFGVIAL.

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

Description:

Beta Defensin-14 Mouse Recombinant

Beta-defensin 14, BD-14, mBD-14, Defensin, beta 14, Defb14.

Product # :

CYT-945

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Quantity :

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Shipped at Room temp

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Description

Beta Defensin-14 Mouse Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 45 amino acids and having a molecular mass of 5.2kDa.The BD14 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BD-14 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
Alpha and Beta Defensins are cationic peptides with antimicrobial activity against Gram-negative and Gram-positive bacteria, fungi and enveloped viruses. These 2-6kDa proteins have vital roles in innate immune system. Mammalian Defensins are classified into alpha, beta and theta categories, based on their size and pattern of disulfide bonding. Beta-Defensins contain a six-cysteine motif which forms 3 intra-molecular disulfide bonds. Since beta-defensins are cationic peptides, they can therefore interact with the membrane of invading microbes, which are negative due to lipopolysaccharides (LPS) and lipoteichoic acid (LTA) found in the cell membrane. In addition, they can affect the stability of the membrane.
Synonyms
Beta-defensin 14, BD-14, mBD-14, Defensin, beta 14, Defb14.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Mouse BD14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-14 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 BD14 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
FLPKTLRKFF CRIRGGRCAV LNCLGKEEQI GRCSNSGRKC CRKKK.
Background
What is the molecular weight/Mw of BD14 Protein?
BD14 Protein has a total Mw of 5.2kDa.

What is the source or expression system of BD14 Protein?
Escherichia Coli.

What is the Purity of BD14 Protein?
BD14 Protein is >96% pure as determined by SDS-PAGE.

What is the Biological Activity of BD14 Protein?
The biological functionality of BD14 Protein will be determined in the future.

What is the amino acid sequence of BD14 Protein?
FLPKTLRKFF CRIRGGRCAV LNCLGKEEQI GRCSNSGRKC CRKKK.

What applications can BD14 Protein be used in?
BD14 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BD14 Protein?
The endotoxin level is minimal, BD14 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:

GDNF Family Receptor Alpha 3 Human Recombinant, Sf9

GDNF Family Receptor Alpha3, GDNFR-alpha-3, GFR-alpha-3, GDNF Receptor Alpha-3, GDNFR3, GDNF Family Receptor Alpha-3, Glial Cell Line-Derived Neurotrophic Factor Receptor Alpha-3, GPI-Linked Receptor, GFRA3.

Product # :

CYT-1013

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Description

GFRA3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 585 amino acids (32-374) and having a molecular mass of 65.5kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). GFRA3 is fused to a 239 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

GFRA3 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
GDNF Family Receptor Alpha 3 (GFRA3) belongs to the GDNF receptor family. GFRA3 creates a signaling receptor complex with RET tyrosine kinase receptor and binds the ligand, artemin (ARTN).
Synonyms
GDNF Family Receptor Alpha3, GDNFR-alpha-3, GFR-alpha-3, GDNF Receptor Alpha-3, GDNFR3, GDNF Family Receptor Alpha-3, Glial Cell Line-Derived Neurotrophic Factor Receptor Alpha-3, GPI-Linked Receptor, GFRA3.
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
ADPDPLPTES RLMNSCLQAR RKCQADPTCS AAYHHLDSCT SSISTPLPSE EPSVPADCLE AAQQLRNSSL IGCMCHRRMK NQVACLDIYW TVHRARSLGN YELDVSPYED TVTSKPWKMN LSKLNMLKPD SDLCLKFAML CTLNDKCDRL RKAYGEACSG PHCQRHVCLR QLLTFFEKAA EPHAQGLLLC PCAPNDRGCG ERRRNTIAPN CALPPVAPNC LELRRLCFSD PLCRSRLVDF QTHCHPMDIL GTCATEQSRC LRAYLGLIGT AMTPNFVSNV NTSVALSCTC RGSGNLQEEC EMLEGFFSHN PCLTEAIAAK MRFHSQLFSQ DWPHPTFAVM AHQNENLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.
Background
What is the molecular weight/Mw of GFRA3 HUMAN, SF9 Protein?
GFRA3 HUMAN, SF9 Protein has a total Mw of 65.5kDa.

What is the source or expression system of GFRA3 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.
What is the Purity of GFRA3 HUMAN, SF9 Protein?
GFRA3 HUMAN, SF9 Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of GFRA3 HUMAN, SF9 Protein?
The biological functionality of GFRA3 HUMAN, SF9 Protein will be determined in the future.

What is the amino acid sequence of GFRA3 HUMAN, SF9 Protein?
ADPDPLPTES RLMNSCLQAR RKCQADPTCS AAYHHLDSCT SSISTPLPSE EPSVPADCLE AAQQLRNSSL IGCMCHRRMK NQVACLDIYW TVHRARSLGN YELDVSPYED TVTSKPWKMN LSKLNMLKPD SDLCLKFAML CTLNDKCDRL RKAYGEACSG PHCQRHVCLR QLLTFFEKAA EPHAQGLLLC PCAPNDRGCG ERRRNTIAPN CALPPVAPNC LELRRLCFSD PLCRSRLVDF QTHCHPMDIL GTCATEQSRC LRAYLGLIGT AMTPNFVSNV NTSVALSCTC RGSGNLQEEC EMLEGFFSHN PCLTEAIAAK MRFHSQLFSQ DWPHPTFAVM AHQNENLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.

What applications can GFRA3 HUMAN, SF9 Protein be used in?
GFRA3 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GFRA3 HUMAN, SF9 Protein?
The endotoxin level is minimal, GFRA3 HUMAN, SF9 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:

Tumor Necrosis Factor-alpha, Mouse-Anti Human

TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

Product # :

ANT-124

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Shipped at Room temp

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formulation
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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesisand viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.
Synonyms
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human TNF-a.
Ig Subclass
Mouse IgG1.
Clone
NYRhTNFa-E2.
Applications
Direct ELISA, Western Blot, Immuneprecipitation, Intracellular staining.
Note
This antibody will bind very well to protein A in a buffer (PBS) containing high salt concentration (3M Nacl).
Titer
In direct ELISA, using alkaline phosphatase goat anti-mouse Ig (Jackson Laboratories) 1:10,000 dilution will yield 0.7 O.D within 10 minutes.
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.
Purification Method
ion exchange.

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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