Search: 1000 results found for "beta-ngf"

Description:

Interferon-gamma, Mouse Anti-Human

Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.

Product # :

ANT-123

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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons.
Synonyms
Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human IFN-g.
Ig Subclass
Mouse IgG2a.
Clone
NYRhIFNg.
Titer
This antibody loses its antigen binding capacity when immobilized on plastic. Biological activity is determined by virus neutralization assay and MHC class II induction.
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20C.
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.

Description:

NCK Adaptor Protein 2 Human Recombinant

NCK Adaptor Protein 2, Growth Factor Receptor-Bound Protein 4, SH2/SH3 Adaptor Protein NCK-Beta, Noncatalytic Region Of Tyrosine Kinase Beta, Cytoplasmic Protein NCK2, GRB4, NCKbeta, Nck-2.

Product # :

PRO-1621

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Description

NCK2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 403 amino acids (1-380) and having a molecular mass of 45.3kDa.NCK2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The NCK2 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 30% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
NCK2 belongs to the NCK family of adaptor proteins. NCK2 holds one SH2 domain and three SH3 domains. NCK2 bind and recruit several proteins that take part in the regulation of receptor protein tyrosine kinases even though it has no known catalytic function. That indicates that NCK2 takes part in cytoskeletal reorganization. Alternate transcription splice variants, encoding diverse isoforms, were characterized.
Synonyms
NCK Adaptor Protein 2, Growth Factor Receptor-Bound Protein 4, SH2/SH3 Adaptor Protein NCK-Beta, Noncatalytic Region Of Tyrosine Kinase Beta, Cytoplasmic Protein NCK2, GRB4, NCKbeta, Nck-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 MGSMTEEVIV IAKWDYTAQQ DQELDIKKNE RLWLLDDSKT WWRVRNAANR TGYVPSNYVE RKNSLKKGSL VKNLKDTLGL GKTRRKTSAR DASPTPSTDA EYPANGSGAD RIYDLNIPAF VKFAYVAERE DELSLVKGSR VTVMEKCSDG WWRGSYNGQI GWFPSNYVLE EVDEAAAESP SFLSLRKGAS LSNGQGSRVL HVVQTLYPFS SVTEEELNFE KGETMEVIEK PENDPEWWKC KNARGQVGLV PKNYVVVLSD GPALHPAHAP QISYTGPSSS GRFAGREWYY GNVTRHQAEC ALNERGVEGD FLIRDSESSP SDFSVSLKAS GKNKHFKVQL VDNVYCIGQR RFHTMDELVE HYKKAPIFTS EHGEKLYLVR ALQ

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:

Cerebral Neurotrophic Factor Human Recombinant

Cerebral neurotrophic factor, arginine-rich, mutated in early stage tumors-like 1, Conserved neurotrophic factor, ARMET-like protein 1, ARMETL1.

Product # :

CYT-167

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Description

CDNF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 161 amino acids and having a molecular mass of 18.5kDa.The CDNF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CDNF protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

Purity

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

Biological Activity

The ED50 as determined by its ability to stimulate the proliferation of rat C6 cells is 15-25µg/ml, corresponding to a specific activity of 40-67units/mg.

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Introduction
CDNF is a member of the ARMET family and acts as a trophic factor for neurons. CDNF inhibits the (6-OHDA)-induced degeneration of neurons. When CDNF controlled after 6-OHDA-lesioning, it reestablishes the function and inhibits the degeneration of neurons in substantia nigra. CDNF is universally expressed in neuronal and non-neuronal tissues. The highest levels in the brain are found in the optic nerve and corpus callosum.
Synonyms
Cerebral neurotrophic factor, arginine-rich, mutated in early stage tumors-like 1, Conserved neurotrophic factor, ARMET-like protein 1, ARMETL1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CDNF 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 CDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QEAGGRPGAD CEVCKEFLNR FYKSLIDRGV NFSLDTIEKE LISFCLDTKG KENRLCYYLG ATKDAATKIL SEVTRPMSVH MPAMKICEKL KKLDSQICEL KYEKTLDLAS VDLRKMRVAE LKQILHSWGE ECRACAEKTD YVNLIQELAP KYAATHPKTE L
Background
Cerebral Neurotrophic Factor Human Recombinant: A Leap Forward in Neurobiology
The field of neurobiology is replete with wonder, particularly due to the influential role of neurotrophic factors. These essential proteins, responsible for the survival and growth of neurons, have become a focal point in modern research. Among these, the Cerebral Neurotrophic Factor (CNF) stands out, offering novel insights and potential breakthroughs in our understanding of neurological health.
Enter the world of bioengineering, a scientific arena where we have successfully replicated CNF, leading to the birth of Cerebral Neurotrophic Factor Human Recombinant (CNF-HR). This is a massive step towards conquering neurodegenerative disorders such as Alzheimer's and Parkinson's diseases, conditions that have perplexed scientists and clinicians for decades.
The extraordinary capacity of CNF-HR lies in its dual functionality - it acts as a defender and a promoter. It defends neurons from harmful degenerative processes while promoting their growth and development. Picture a devoted gardener who tirelessly protects his garden from pests and nurtures the growth of each plant. In this context, the brain is the vibrant garden, and the neurons, the delicate plants we must care for.
Although this scientific breakthrough sparks enthusiasm, it's crucial to remember the challenges that lie ahead. The path to determining the most effective method of delivering CNF-HR to the brain, identifying the optimal dosage, and monitoring potential side effects is a winding one. Nevertheless, with continuous research and relentless scientific curiosity, we are optimistic about overcoming these challenges.
In conclusion, the development of CNF-HR is a significant milestone in the fascinating journey of neurobiology. Its potential to change the trajectory of treating neurodegenerative diseases and enhancing our understanding of neuronal function is tremendous. While the journey is strewn with complexities, the potential rewards we stand to reap promise a future where neurodegenerative diseases could be effectively managed or even cured.
What is the molecular weight/Mw of CDNF Protein?
CDNF Protein has a total Mw of 18.5kDa.

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

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

What is the Biological Activity of CDNF Protein?
The ED50 as determined by its ability to stimulate the proliferation of rat C6 cells is 15-25µg/ml, corresponding to a specific activity of 40-67units/mg.

What is the amino acid sequence of CDNF Protein?
QEAGGRPGAD CEVCKEFLNR FYKSLIDRGV NFSLDTIEKE LISFCLDTKG KENRLCYYLG ATKDAATKIL SEVTRPMSVH MPAMKICEKL KKLDSQICEL KYEKTLDLAS VDLRKMRVAE LKQILHSWGE ECRACAEKTD YVNLIQELAP KYAATHPKTE L

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

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

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

Description:

Insulin Like Growth Factor-1, Mutant E3R Human Recombinant

Insulin-Like Growth Factor-1.

Product # :

CYT-1217

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Description

IGF1 E3R Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids (Gly49-Ala118) and having a molecular mass of 8.6kDa. IGF1 E3R Human is fused to a 6 a.a his tag at C-Terminus and is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The filtered (0.4µm) concentrated protein solution was lyophilized from 0.5mg/ml solution in 50 mM NaCl, 20 mM Tris and 5% (w/v) trehalose, pH 8.0.

Purity

Greater than 95% as determined by SDS-PAGE.

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Synonyms
Insulin-Like Growth Factor-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. IGF1 E3R is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MGPRTLCGAE LVDALQFVCG DRGFYFNKPT GYGSSSRRAP QTGIVDECCF RSCDLRRLEM YCAPLKPAKS AHHHHHH.
Background
Insulin-like Growth Factor 1 (IGF-1) is a critical peptide hormone that plays a central role in regulating growth and development. Genetic mutations in the IGF-1 gene can result in altered IGF-1 variants, leading to various physiological consequences. Understanding these IGF-1 mutants is of paramount importance as they offer insights into growth disorders, metabolic regulation, and potential therapeutic avenues. This research delves into the world of IGF-1 mutants, shedding light on their diverse functions and implications for human health.
The primary objective of this research is to elucidate the impact of IGF-1 mutations on growth regulation. In vitro and in vivo experiments will be conducted to investigate how these mutants interact with IGF-1 receptors, influence downstream signaling pathways, and modulate growth plate dynamics. Understanding these mechanisms is crucial for unraveling the complexities of growth disorders associated with IGF-1 mutations.
The second objective is to assess the clinical relevance of IGF-1 mutants in growth-related conditions. Clinical studies involving individuals with growth hormone deficiencies or growth disorders linked to IGF-1 mutations will be conducted to evaluate the effects of these mutants on stature and overall health. These investigations may provide valuable insights into potential therapeutic strategies for individuals affected by growth-related disorders.
The third objective is to explore the broader implications of IGF-1 mutants in metabolic regulation and age-related conditions. Research will investigate their roles in metabolic homeostasis, longevity, and susceptibility to age-related diseases. Understanding the multifaceted properties of IGF-1 mutants may open new avenues for therapeutic interventions in various health and aging-related conditions.
By delving into the diverse functions of IGF-1 mutants, this research aims to expand our understanding of their physiological roles and clinical applications. The findings may contribute to the development of targeted interventions for growth disorders, metabolic conditions, and age-related 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:

Mouse Anti Shiga Like Toxin 1B

Product # :

ANT-660

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Description

Shiga like toxin 1B monoclonal antibody IgG1 derived from mouse, immunized with recombinant Shiga-like toxin 1 subunit B ( E. coli O157:H7). The subunit B has nontoxic action and is a functional region which binds to the receptor. Shiga-like toxin 1 subunit B contains amino acid from 2 to 90 of Shiga-like toxin 1subunit B, it forms pentamer binding to the host cell receptor.

Formulation

1x PBS and 0.05% sodium nitrate.

Purity

Greater than 95% as determined by 12% PAGE (coomassie staining).

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Introduction
Shiga-like toxin (verotoxin) is a toxin produced by some strains of Escherichia coli. Shiga-like toxin is named for its similarity to the AB5-type Shiga toxin produced by the bacteria Shigella dysenteriae. There are two known types-SLT1 and SLT2. The Shiga-like toxin is linked with hemolytic-uremic syndrome. Shiga-like toxin requires highly specific receptors on the cells'' surface in order to attach and enter the cell. Species such as cattle, swine, and deer which do not carry these receptors may harbor toxigenic bacteria without any ill effect, dropping them in their feces, from where they may be distributed to humans. Shiga Like Toxin-1 Subunit B has nontoxic action, it is the functional region which binds to the receptor. The Shiga Like Toxin-1 Subunit B can be useful in vaccine study, antibody test and other functional research.
Physical Appearance
Sterile Filtered clear colorless solution.
Stability
Shiga like toxin 1B monoclonal antibody although stable at 4°C for 1 week, should be stored 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.
Type
Mouse antibody Monoclonal.

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:

Zika Envelope Full Length Protein Recombinant

Product # :

ZKV-007

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Description

The E.Coli derived Recombinant Zika Envelope protein 40-400 a.a. having an Mw of 45kDa. The Zika Envelope full length protein without a C-terminal hydrophobic region. The Zika Envelope full length protein is fused to a 6xHis tag at C-terminus and purified by proprietary chromatographic technique.

Source

Escherichia Coli.

Formulation

Zika Envelope protein solution contains PBS and 25mM arginine.

Purity

Zika Envelope protein is >95% pure as determined by SDS-PAGE.

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Introduction
Zika virus (ZIKV) belongs to the family Flaviviridae and the genus Flavivirus, it is transmitted by daytime-active Aedes mosquitoes, such as A. aegypti and A. albopictus. The Zika virus is related to the dengue, yellow fever, Japanese encephalitis, and West Nile viruses. Much like the other flaviviruses, Zika virus is enveloped and icosahedral and has a nonsegmented, single-stranded, positive-sense RNA genome. Zika fever is an infection, which often causes no symptoms or only mild ones, like a mild form of dengue fever, and it is treated by rest. As of February 2016, there has been mounting evidence that Zika fever in pregnant women can cause abnormal brain development in their fetuses by mother-to-child transmission, which may result in miscarriage or microcephaly, however it is not yet known whether Zika virus causes microcephaly. Furthermore, a connection has been established with neurologic conditions in infected adults, including Guillain–Barre syndrome.
Physical Appearance
Sterile Filtered solution.
Stability
Zika Envelope protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Applications
ELISA, rapid test and immunoassay.

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:

Flt3 Ligand Mouse Recombinant, Sf9

Fms-related tyrosine kinase 3 ligand, Flt3 ligand, Flt3L, SL cytokine, lt3lgF, Flt3l.

Product # :

CYT-910

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Description

Flt3 Ligand produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (27-189 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 169 amino acids and having a molecular mass of 19.3kDa.Flt3 Ligand shows multiple bands between 18-28kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

Flt3 Ligand protein solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.
Synonyms
Fms-related tyrosine kinase 3 ligand, Flt3 ligand, Flt3L, SL cytokine, lt3lgF, Flt3l.
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
GTPDCYFSHS PISSNFKVKF RELTDHLLKD YPVTVAVNLQ DEKHCKALWS LFLAQRWIEQ LKTVAGSKMQ TLLEDVNTEI HFVTSCTFQP LPECLRFVQT NISHLLKDTC TQLLALKPCI GKACQNFSRC LEVQCQPDSS TLLPPRSPIA LEATELPEPR PRQHHHHHH
Background
What is the molecular weight/Mw of FLT3 LIGAND MOUSE, SF9 Protein?
FLT3 LIGAND MOUSE, SF9 Protein has a total Mw of 19.3kDa.

What is the source or expression system of FLT3 LIGAND MOUSE, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of FLT3 LIGAND MOUSE, SF9 Protein?
FLT3 LIGAND MOUSE, SF9 Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of FLT3 LIGAND MOUSE, SF9 Protein?
The biological functionality of FLT3 LIGAND MOUSE, SF9 Protein will be determined in the future.

What is the amino acid sequence of FLT3 LIGAND MOUSE, SF9 Protein?
GTPDCYFSHS PISSNFKVKF RELTDHLLKD YPVTVAVNLQ DEKHCKALWS LFLAQRWIEQ LKTVAGSKMQ TLLEDVNTEI HFVTSCTFQP LPECLRFVQT NISHLLKDTC TQLLALKPCI GKACQNFSRC LEVQCQPDSS TLLPPRSPIA LEATELPEPR PRQHHHHHH.

What applications can FLT3 LIGAND MOUSE, SF9 Protein be used in?
FLT3 LIGAND MOUSE, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FLT3 LIGAND MOUSE, SF9 Protein?
The endotoxin level is minimal, FLT3 LIGAND MOUSE, 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:

Nucleotide Binding Protein 2 Human Recombinant

Nucleotide Binding Protein 2, Nucleotide Binding Protein 2 (MinD Homolog, E. Coli), NBP 2,CFD1, C447E6.1 (Nucleotide Binding Protein 1 (E.Coli MinD Like) ), Homolog Of Yeast Cytosolic Fe-S Cluster Deficient 1, Nucleotide Binding Protein 2 (E.Coli MinD Like), Cytosolic Fe-S Cluster Assembly Factor NUBP2, Nucleotide-Binding Protein 2, NUBP1, NUBP2.

Product # :

PRO-2133

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Description

NUBP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 294 amino acids (1-271 a.a) and having a molecular mass of 31.2kDa.NUBP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

NUBP2 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 50% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Nucleotide Binding Protein 2, also known as NUBP2 is an adenosine triphosphate (ATP) as well as metal-binding protein which is essential for the assembly of cyotosolic iron-sulfur proteins. NUBP2 performs in a heterotetramer with nucleotide-binding protein 1 (NUBP1). Moreover, alternative splicing results in multiple transcript variants have been found for NUBP2.
Synonyms
Nucleotide Binding Protein 2, Nucleotide Binding Protein 2 (MinD Homolog, E. Coli), NBP 2,CFD1, C447E6.1 (Nucleotide Binding Protein 1 (E.Coli MinD Like) ), Homolog Of Yeast Cytosolic Fe-S Cluster Deficient 1, Nucleotide Binding Protein 2 (E.Coli MinD Like), Cytosolic Fe-S Cluster Assembly Factor NUBP2, Nucleotide-Binding Protein 2, NUBP1, NUBP2.
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 MGSMEAAAEP GNLAGVRHII LVLSGKGGVG KSTISTELAL ALRHAGKKVG ILDVDLCGPS IPRMLGAQGR AVHQCDRGWA PVFLDREQSI SLMSVGFLLE KPDEAVVWRG PKKNALIKQF VSDVAWGELD YLVVDTPPGT SDEHMATIEA LRPYQPLGAL VVTTPQAVSV GDVRRELTFC RKTGLRVMGI VENMSGFTCP HCTECTSVFS RGGGEELAQL AGVPFLGSVP LDPALMRTLE EGHDFIQEFP GSPAFAALTS IAQKILDATP ACLP

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:

Serine/arginine-Rich Splicing Factor 1 Human Recombinant, Sf9

SRSF1, ASF, SF2, SF2p33, SFRS1, Splicing Factor, Arginine/Serine-Rich, 30-KD, A, Alternate Splicing Factor, SRp30a, ASF-1, Serine And Arginine Rich Splicing Factor 1, Pre-MRNA-Splicing Factor SF2, P33 Subunit, Splicing Factor, Arginine/Serine-Rich 1, Serine/Arginine-Rich Splicing Factor 1, Alternative-Splicing Factor 1, SR Splicing Factor 1, Splicing Factor 2.

Product # :

PRO-2417

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Description

SRSF1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 254 amino acids (1-248) and having a molecular mass of 28.5kDa. SRSF1 is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

SRSF1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 100mM KCl, 1mM DTT, 0.2mM EDTA and 40% Glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Serine/arginine-rich splicing factor 1 (SFRS1) belongs to the arginine/serine-rich splicing factor protein family, and functions in both constitutive and alternative pre-mRNA splicing. SFRS1 binds to pre-mRNA transcripts and components of the spliceosome, and can either initiate or inhibit splicing depending on the position of the pre-mRNA binding site. The ability of SFRS1 to activate splicing is controlled by phosphorylation and interactions with other splicing factor associated proteins.
Synonyms
SRSF1, ASF, SF2, SF2p33, SFRS1, Splicing Factor, Arginine/Serine-Rich, 30-KD, A, Alternate Splicing Factor, SRp30a, ASF-1, Serine And Arginine Rich Splicing Factor 1, Pre-MRNA-Splicing Factor SF2, P33 Subunit, Splicing Factor, Arginine/Serine-Rich 1, Serine/Arginine-Rich Splicing Factor 1, Alternative-Splicing Factor 1, SR Splicing Factor 1, Splicing Factor 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
MSGGGVIRGP AGNNDCRIYV GNLPPDIRTK DIEDVFYKYG AIRDIDLKNR RGGPPFAFVE FEDPRDAEDA VYGRDGYDYD GYRLRVEFPR SGRGTGRGGG GGGGGGAPRG RYGPPSRRSE NRVVVSGLPP SGSWQDLKDH MREAGDVCYA DVYRDGTGVV EFVRKEDMTY AVRKLDNTKF RSHEGETAYI RVKVDGPRSP SYGRSRSRSR SRSRSRSRSN SRSRSYSPRR SRGSPRYSPR HSRSRSRTHH 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:

CD55 Mouse Recombinant

Complement decay-accelerating factor, GPI-anchored, DAF-GPI, CD_antigen: CD55.

Product # :

PRO-2319

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Description

CD55 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 336 amino acids (35-362 a.a.) and having a molecular mass of 36.8kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). CD55 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

CD55 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
CD55 belongs to the RCA (regulators of complement activation) family characterized by 4-30 SCRs (short consensus repeats) in their plasma-exposed regions. CD55 is widely expressed in malignant tumors and nevertheless functions as an inhibitor of the complement system.
Synonyms
Complement decay-accelerating factor, GPI-anchored, DAF-GPI, CD_antigen: CD55.
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
DCGPPPDIPN ARPILGRHSK FAEQSKVAYS CNNGFKQVPD KSNIVVCLEN GQWSSHETFC EKSCVAPERL SFASLKKEYL NMNFFPVGTI VEYECRPGFR KQPPLPGKAT CLEDLVWSPV AQFCKKKSCP NPKDLDNGHI NIPTGILFGS EINFSCNPGY RLVGVSSTFC SVTGNTVDWD DEFPVCTEIH CPEPPKINNG IMRGESDSYT YSQVVTYSCD KGFILVGNAS IYCTVSKSDV GQWSSPPPRC IEKSKVPTKK PTINVPSTGT PSTPQKPTTE SVPNPGDQPT PQKPSTVKVS ATQHVPVTKT TVRHPIRTST DKGEPNTGLE HHHHHH.

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

Description:

Growth Hormone Binding Protein Human Recombinant, Sf9

GHR, GHBP, GHIP.

Product # :

CYT-1152

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Description

GHBP Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 254 amino acids (19-264aa) and having a molecular mass of 29.4kDa.GHBP is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The GHBP solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Measured by ability to inhibit GH-induced proliferation assay using Nb2-11 Rat lymphoma cells in the presence of 1.25ng/ml of human growth hormone. The ED50 for this effect is equal or less than 10ng/ml.

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Introduction
Growth Hormone Binding Protein or GHR, is a protein, part of the cytokine receptor superfamily. GHR binds to 2 receptors, therefore it enhances signal transduction via dimerization of receptors. In elevated levels, growth hormone operates as an antagonist due to high variance in the binding sites affinities. The antagonist operation can be embellished even more when the binding site is reduced its affinity.
Synonyms
GHR, GHBP, GHIP.
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
FSGSEATAAI LSRAPWSLQS VNPGLKTNSS KEPKFTKCRS PERETFSCHW TDEVHHGTKN LGPIQLFYTR RNTQEWTQEW KECPDYVSAG ENSCYFNSSF TSIWIPYCIK LTSNGGTVDE KCFSVDEIVQ PDPPIALNWT LLNVSLTGIH ADIQVRWEAP RNADIQKGWM VLEYELQYKE VNETKWKMMD PILTTSVPVY SLKVDKEYEV RVRSKQRNSG NYGEFSEVLY VTLPQMSQFT
CEEDFYLEHH 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:

Biglycan Mouse Recombinant

BGN, DSPG1, MRLS, PG-S1, PGI, SEMDX, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, Biglycan Proteoglycan, MRLS.

Product # :

PRO-2537

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Description

BGN produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 574 amino acids (38-369 a.a.) and having a molecular mass of 64.6kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). BGN is expressed with a 242 hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

The BGN solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Biglycan (BGN) is a small cellular or pericellular matrix proteoglycan which takes part in assembly of collagen fibrils and muscle regeneration. BGN is closely correlated in structure to two other small proteoglycans, decorin and fibromodulin. BGN interacts with several proteins involved in muscular dystrophy, including alpha-dystroglycan, alpha- and gamma-sarcoglycan and collagen VI. BGN is also critical for the assembly of the dystrophin-associated protein complex.
Synonyms
BGN, DSPG1, MRLS, PG-S1, PGI, SEMDX, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, Biglycan Proteoglycan, MRLS.
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
ADPDEEASGS DTTSGVPDLD SVTPTFSAMC PFGCHCHLRV VQCSDLGLKT VPKEISPDTT LLDLQNNDIS ELRKDDFKGL QHLYALVLVN NKISKIHEKA FSPLRKLQKL YISKNHLVEI PPNLPSSLVE LRIHDNRIRK VPKGVFSGLR NMNCIEMGGN PLENSGFEPG AFDGLKLNYL
RISEAKLTGI PKDLPETLNE LHLDHNKIQA IELEDLLRYS KLYRLGLGHN QIRMIENGSL SFLPTLRELH LDNNKLSRVP AGLPDLKLLQ VVYLHSNNIT KVGINDFCPM GFGVKRAYYN GISLFNNPVP YWEVQPATFR CVTDRLAIQF GNYKKLEPKS CDKTHTCPPC PAPELLGGPS
VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGKHH 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:

Glial Fibrillary Acidic Protein Bovine

Glial fibrillary acidic protein, GFAP.

Product # :

PRO-2784

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Description

GFAP Bovine having a calculated molecular mass of 52 kDa, pI-5.4.

Source

Bovine spinal cord.

Formulation

GFAP was lyophilized from a 1mg/ml solution containing 10mM sodium phosphate buffer pH 7.5, 6M urea, 1mM EDTA, 2mM DTT and 10mM methylammonium chloride.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Synonyms
Glial fibrillary acidic protein, GFAP.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Store the lyophilized GFAP between 2-8°C, do not freeze. Upon reconstitution GFAP should be stored at -20°C. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized GFAP in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
Glial fibrillary acidic protein (GFAP) is a key intermediate filament protein found predominantly in astrocytes, a type of glial cell in the central nervous system. While extensive research has been conducted on GFAP in rodents and humans, the study of GFAP in bovine brain tissue is an emerging area with potential for advancing our understanding of astrocytic function and neurological health in larger mammals. Bovine brains provide a unique model system due to their size and complexity, making them valuable for investigating astrocyte-specific functions. This research aims to provide a comprehensive exploration of GFAP in bovine brain tissue, shedding light on its functions and implications for neurological health.
The primary objective of this research is to elucidate the role of GFAP in bovine brain tissue, particularly in astrocyte structure and function. In vitro and ex vivo experiments, utilizing bovine astrocyte cultures and brain tissue slices, will be conducted to investigate how GFAP contributes to astrocytic morphology, intracellular signaling, and response to neuronal injury or disease. Understanding these mechanisms is fundamental for deciphering the complexities of astrocyte biology in large mammalian brains.
The second objective is to assess the relevance of bovine GFAP in neurodegenerative diseases and brain injuries. Studies involving bovine brain models of neurodegenerative conditions such as Alzheimer's disease or traumatic brain injury will be conducted to evaluate the role of GFAP in disease progression, neuroinflammation, and tissue repair. These investigations may provide valuable insights into potential therapeutic strategies for neurological disorders.
The third objective is to explore the potential applications of bovine GFAP in biotechnology and medical research. Research will investigate the use of bovine astrocyte cultures as models for studying astrocyte-neuron interactions and for developing tissue engineering approaches for neurological repair and regeneration.
By delving into the functions and roles of GFAP in bovine brain tissue, this research aims to expand our knowledge of astrocyte biology, its implications for neurological health, and its potential applications in biotechnology and medical research.

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

Description:

GTP-Binding Protein SAR1B Human Recombinant

GTP-binding protein SAR1b, GTP-binding protein B, GTBPB, SAR1B, SARA2, SARB, ANDD, CMRD.

Product # :

PRO-310

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Description

SAR1B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 221 amino acids (1-198 a.a) and having a molecular mass of 24.8kDa.SAR1B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SAR1B protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
SAR1B is a small GTPase that functions as a homodimer. GTP-Binding Protein SAR1B (SAR1b) is involved in transport from the endoplasmic reticulum to the Golgi apparatus and also in the selection of the protein cargo and the assembly of the COPII coat complex. The SAR1B protein is activated by the guanine nucleotide exchange factor PREB. SAR1B gene defects are a cause of chylomicron retention disease (CMRD), also known as Anderson disease (ANDD).
Synonyms
GTP-binding protein SAR1b, GTP-binding protein B, GTBPB, SAR1B, SARA2, SARB, ANDD, CMRD.
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 MGSMSFIFDW IYSGFSSVLQ FLGLYKKTGK LVFLGLDNAG KTTLLHMLKD DRLGQHVPTL HPTSEELTIA GMTFTTFDLG GHVQARRVWK NYLPAINGIV FLVDCADHER LLESKEELDS LMTDETIANV PILILGNKID RPEAISEERL REMFGLYGQT TGKGSISLKE LNARPLEVFM CSVLKRQGYG EGFRWMAQYI D.

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:

SLAMF6 Human Recombinant

CD352, KALI, KALIb, Ly108, NTB-A, NTBA, Activating NK receptor, SLAM family member 6.

Product # :

PRO-1286

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Description

SLAMF6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 228 amino acids (22-226 a.a.) and having a molecular mass of 25.5kDa. SLAMF6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SLAMF6 protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
SLAM family member 6 (SLAMF6) is a member of the SLAM family of immune cell receptors. SLAMF6 is a unique receptor on T cells which, when triggered potentiates T cell expansion in a CD28-independent manner. SLAMF6 has a high expression on NK-, T-, and B cells. SLAMF6 exhibits homotypic interactions and can connect with adaptor molecules such as SAP to alter immune cell function.
Synonyms
CD352, KALI, KALIb, Ly108, NTB-A, NTBA, Activating NK receptor, SLAM family member 6.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSQSSLTPL MVNGILGESV TLPLEFPAGE KVNFITWLFN ETSLAFIVPH ETKSPEIHVT NPKQGKRLNF TQSYSLQLSN LKMEDTGSYR AQISTKTSAK LSSYTLRILR QLRNIQVTNH SQLFQNMTCE LHLTCSVEDA DDNVSFRWEA LGNTLSSQPN LTVSWDPRIS SEQDYTCIAE NAVSNLSFSV SAQKLCEDVK IQYTDTKM.

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

Description:

Insulin-Like Growth Factor Binding Protein-1 Human Recombinant

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

Product # :

CYT-299

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Description

IGFBP-1 Human Recombinant (26-259 a.a.) produced in NS0 is a single, glycosylated, polypeptide chain containing 234 amino acids and having a molecular mass of 25kDa. The IGFBP1 is purified by proprietary chromatographic techniques.

Source

Mouse myeloma cell line, NS0.

Formulation

IGFBP-1 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as determined by the inhibition of rHuIGF-I-induced proliferation of human MCF-7 cells, is less than 4µg/ml.

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Introduction
IGFBP1 is a member of the insulin-like growth factor binding protein (IGFBP) family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein binds both insulin-like growth factors (IGFs) I and II and circulates in the plasma. Binding of this protein prolongs the half-life of the IGFs and alters their interaction with cell surface receptors. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
Synonyms
IBP-1, IGF-Binding Protein 1, AFBP, PP12, IGF-BP25, hIGFBP-1, IGFBP-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IGFBP1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF-BP1 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 IBP-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APWQCAPCSA EKLALCPPVS ASCSEVTRSA GCGCCPMCAL PLGAACGVAT ARCARGLSCR ALPGEQQPLH ALTRGQGACV QESDASAPHA AEAGSPESPE STEITEEELL DNFHLMAPSE EDHSILWDAI STYDGSKALH VTNIKKWKEP CRIELYRVVE SLAKAQETSG EEISKFYLPN CNKNGFYHSR QCETSMDGEA GLCWCVYPWN GKRIPGSPEI RGDPNCQIYF NVQN.

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:

JAZF zinc finger 1 Human Recombinant

Juxtaposed with another zinc finger protein 1 , TAK1-interacting protein 27, Zinc finger protein 802, JAZF1, TIP27, ZNF802, JAZF zinc finger 1, Juxtaposed With Another Zinc Finger Gene 1.

Product # :

PRO-1444

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Description

JAZF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 266 amino acids (1-243 a.a) and having a molecular mass of 29.5kDa.JAZF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

JAZF1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
JAZF zinc finger 1 (JAZF1) is a nuclear protein with 3 C2H2-type zinc fingers, which functions as a transcriptional repressor. Chromosomal anomalies involving the JAZF1 are linked with endometrial stromal tumors. Alternatively spliced variants which encode different protein isoforms have been described; though, not all variants have been fully characterized.
Synonyms
Juxtaposed with another zinc finger protein 1 , TAK1-interacting protein 27, Zinc finger protein 802, JAZF1, TIP27, ZNF802, JAZF zinc finger 1, Juxtaposed With Another Zinc Finger Gene 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 MGSMTGIAAA SFFSNTCRFG GCGLHFPTLA DLIEHIEDNH IDTDPRVLEK QELQQPTYVA LSYINRFMTD AARREQESLK KKIQPKLSLT LSSSVSRGNV STPPRHSSGS LTPPVTPPIT PSSSFRSSTP TGSEYDEEEV DYEESDSDES WTTESAISSE AILSSMCMNG GEEKPFACPV PGCKKRYKNV NGIKYHAKNG HRTQIRVRKP FKCRCGKSYK TAQGLRHHTI NFHPPVSAEI IRKMQQ

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

Description:

Placental Growth Factor-3 Human Recombinant, sf9

Placental Growth Factor, Placental Growth Factor Vascular Endothelial Growth Factor-Related Protein, PGFL, PLGF, Placental Growth Factor-Like, Placenta Growth Factor, SHGC-10760, D12S1900, PlGF-2, PGF.

Product # :

CYT-961

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Description

PLGF3 Human Recombinant produced in Spodoptera frugiperda is a glycosylated homodimer containing 2 chains of 203 amino acids (Leu19-Arg221) and having a molecular mass of 58kDa.The PLGF-3 is purified by proprietary chromatographic techniques.

Source

Spodoptera frugiperda.

Formulation

PLGF-3 protein was lyophilized from a 0.2µm filtered solution in HCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as measured by its binding ability to rHuVEGF R1 in a functional ELISA, is less than 3ng/ml.

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Introduction
PLGF is a growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration. It binds to receptor vegfr-1/flt1.
Synonyms
Placental Growth Factor, Placental Growth Factor Vascular Endothelial Growth Factor-Related Protein, PGFL, PLGF, Placental Growth Factor-Like, Placenta Growth Factor, SHGC-10760, D12S1900, PlGF-2, PGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PLGF3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PLGF-3 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 PLGF3 in sterile 4mM HCl 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:

G Antigen 2A Human Recombinant

G Antigen 2A, G Antigen 2A/2B, Cancer/Testis Antigen Family 4, Cancer/Testis Antigen Family 4, Member 2, GAGE-2A, Member 2, CT4.2, GAGE-2.

Product # :

PRO-1705

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Description

GAGE2A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 139 amino acids (1-116) and having a molecular mass of 15.2kDa.GAGE2A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GAGE2A solution (0.5mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 20% Glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
GAGE2A is a member of a multigene family expressed in a large variety of tumors while in normal tissues; expression is limited to germ cells. These genes organized in clustered repeats, have a high degree of predicted sequence identity, however differ by scattered single nucleotide change. Their sequences have either the antigenic peptide YRPRPRRY or YYWPRPRRY which is recognized by cytotoxic T-cells.
Synonyms
G Antigen 2A, G Antigen 2A/2B, Cancer/Testis Antigen Family 4, Cancer/Testis Antigen Family 4, Member 2, GAGE-2A, Member 2, CT4.2, GAGE-2.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSWRGRS TYRPRPRRYV EPPEMIGPMR PEQFSDEVEP ATPEEGEPAT QRQDPAAAQE GQDEGASAGQ GPKPEAHSQE QGHPQTGCEC EDGPDGQEMD PPNPEEVKTP EEGEKQSQC

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:

Glycoprotein Nmb Human Recombinant

Transmembrane glycoprotein NMB, Transmembrane glycoprotein HGFIN, GPNMB, HGFIN, NMB, Glycoprotein (transmembrane) nmb.

Product # :

PRO-1666

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Description

GPNMB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 476 amino acids (22-474) and having a molecular mass of 53.2 kDa.GPNMB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Glycoprotein Nmb (GPNMB) is a member of the PMEL/NMB family. GPNMB is a type I transmembrane glycoprotein which exhibits homology to the pMEL17 precursor, a melanocyte-specific protein. GPNMB is expressed in the lowly metastatic human melanoma cell lines and xenografts but has no expression in the highly metastatic cell lines. GPNMB might be involved in growth delay and reduction of metastatic potential. GPNMB is up-regulated in a number of cancer cells, including in glioblastoma multiforme. GPNMB is expressed in many melanoma cells, as well as in tissue macrophages, including liver Kuppfer cells and lung alveolar macrophages, in podocytes and in some cells of the ciliary body of the eye (at protein level). GPNMB is hardly detectable in the healthy brain.
Synonyms
Transmembrane glycoprotein NMB, Transmembrane glycoprotein HGFIN, GPNMB, HGFIN, NMB, Glycoprotein (transmembrane) nmb.
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 MGSAKRFHDV LGNERPSAYM REHNQLNGWS SDENDWNEKL YPVWKRGDMR WKNSWKGGRV QAVLTSDSPA LVGSNITFAV NLIFPRCQKE DANGNIVYEK NCRNEAGLSA DPYVYNWTAW SEDSDGENGT GQSHHNVFPD GKPFPHHPGW RRWNFIYVFH TLGQYFQKLG RCSVRVSVNT ANVTLGPQLM EVTVYRRHGR AYVPIAQVKD VYVVTDQIPV FVTMFQKNDR NSSDETFLKD LPIMFDVLIH DPSHFLNYST INYKWSFGDN TGLFVSTNHT VNHTYVLNGT FSLNLTVKAA APGPCPPPPP PPRPSKPTPS LGPAGDNPLE LSRIPDENCQ INRYGHFQAT ITIVEGILEV NIIQMTDVLM PVPWPESSLI DFVVTCQGSI PTEVCTIISD PTCEITQNTV CSPVDVDEMC LLTVRRTFNG SGTYCVNLTL GDDTSLALTS TLISVP.

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:

Zinc Finger Protein 689 Human Recombinant

Zinc Finger Protein 689, Transcription-Involved Protein Upregulated in HCC 1, TIPUH1.

Product # :

PRO-1737

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Description

ZNF689 Human Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 523 amino acids (1-500a.a) and having a molecular mass of 59.3kDa.ZNF689 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ZNF689 protein solution (1.0mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Zinc Finger Protein 689 (ZNF689) is a member of the krueppel C2H2-type zinc-finger protein family. The ZNF689 protein contains 12 C2H2-type zinc fingers and 1 KRAB domain. ZNF689 may be involved in transcriptional regulation.
Synonyms
Zinc Finger Protein 689, Transcription-Involved Protein Upregulated in HCC 1, TIPUH1.
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 MGSMAPPSAP LPAQGPGKAR PSRKRGRRPR ALKFVDVAVY FSPEEWGCLR PAQRALYRDV MRETYGHLGA LGCAGPKPAL ISWLERNTDD WEPAALDPQE YPRGLTVQRK SRTRKKNGEK EVFPPKEAPR KGKRGRRPSK PRLIPRQTSG GPICPDCGCT FPDHQALESH KCAQNLKKPY PCPDCGRRFS YPSLLVSHRR AHSGECPYVC DQCGKRFSQR KNLSQHQVIH TGEKPYHCPD CGRCFRRSRS LANHRTTHTG EKPHQCPSCG RRFAYPSLLA IHQRTHTGEK PYTCLECNRR FRQRTALVIH QRIHTGEKPY PCPDCERRFS SSSRLVSHRR VHSGERPYAC EHCEARFSQR STLLQHQLLH TGEKPYPCPD CGRAFRRSGS LAIHRSTHTE EKLHACDDCG RRFAYPSLLA SHRRVHSGER PYACDLCSKR FAQWSHLAQH QLLHTGEKPF PCLECGRCFR QRWSLAVHKC SPKAPNCSPR SAIGGSSQRG NAH.

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:

Neurotrophin-1 Human Recombinant

Cardiotrophin-Like Cytokine Factor 1, Novel Neurotrophin-1 , BSF3, CLC, CRLF1 Associated Cytokine-Like Factor 1, B-Cell Stimulating Factor 3, B-Cell-Stimulating Factor 3, BSF-3, NNT-1, NNT1, Neurotrophin-1/B-Cell Stimulating Factor-3, Cold-Induced Sweating Syndrome 2, B-Cell Stimulatory Factor 3, CISS2, NR6, CLCF1.

Product # :

CYT-869

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
source
formulation
purity
biological activity
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Description

Neurotrophin-1 Human Recombinant (28-225) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 199 amino acids and having a molecular mass of 22kDa.The NNT-1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

NNT-1 protein was lyophilized from a 0.2µm filtered solution in Acetonitrile and TFA.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as measured in a cell proliferation assay using human TF?1 cells transfected with human CNTF R?, is less than 15ng/ml.

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Introduction
Cardiotrophin-like cytokine (CLC/ NNT-1) belongs to the IL-6 family of cytokines. All family members share the receptor subunit gp130, which belongs to the type I cytokine receptor superfamily. NNT1 is a trophic factor for motor neurons, a stimulator of ACTH release from corticotrophs, and an inducer of IgE synthesis and B cell proliferation. Cells expressing NNT-1 include embryonic muscle, lung epithelium, and mesenchyme. NNT1 binds to and activates the ILST/gp130 receptor.
Synonyms
Cardiotrophin-Like Cytokine Factor 1, Novel Neurotrophin-1 , BSF3, CLC, CRLF1 Associated Cytokine-Like Factor 1, B-Cell Stimulating Factor 3, B-Cell-Stimulating Factor 3, BSF-3, NNT-1, NNT1, Neurotrophin-1/B-Cell Stimulating Factor-3, Cold-Induced Sweating Syndrome 2, B-Cell Stimulatory Factor 3, CISS2, NR6, CLCF1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Neurotrophin-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NNT1 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 NNT1 in sterile 18M-cm H2O not less than 0.5mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MLNRTGDPGP GPSIQKTYDL TRYLEHQLRS LAGTYLNYLG PPFNEPDFNP PRLGAETLPR ATVDLEVWRS LNDKLRLTQN YEAYSHLLCY LRGLNRQAAT AELRRSLAHF CTSLQGLLGS IAGVMAALGY PLPQPLPGTE PTWTPGPAHS DFLQKMDDFW LLKELQTWLW RSAKDFNRLK KKMQPPAAAV TLHLGAHGF.
Background
What is the molecular weight/Mw of CLCF Protein?
CLCF Protein has a total Mw of 22kDa.

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

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

What is the Biological Activity of CLCF Protein?
The ED50, as measured in a cell proliferation assay using human TF?1 cells transfected with human CNTF R?, is less than 15ng/ml.

What is the amino acid sequence of CLCF Protein?
MLNRTGDPGP GPSIQKTYDL TRYLEHQLRS LAGTYLNYLG PPFNEPDFNP PRLGAETLPR ATVDLEVWRS LNDKLRLTQN YEAYSHLLCY LRGLNRQAAT AELRRSLAHF CTSLQGLLGS IAGVMAALGY PLPQPLPGTE PTWTPGPAHS DFLQKMDDFW LLKELQTWLW RSAKDFNRLK KKMQPPAAAV TLHLGAHGF.

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

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

Influenza B Virus Nucleoprotein Recombinant

Product # :

IHA-038

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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description
source
formulation
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Description

Recombinant Influenza B Virus Nucleoprotein produced in E. coli having a Mw of 76.8kDa. IBV-NP is fused to a 6xHis tag at its C terminal is and purified by proprietary chromatographic technique.

Source

E. coli.

Formulation

IBV-NP protein solution contains 25mM K2CO3 and PBS.

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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
HMSNMDIDGMNTGTIDKTPEEITSGTSGTTRPIIRPATLAPPSNKRTRNPSPDRTTTSSE
DDVGRKAQKKQTPTEIKKSVYNMVVKLGEFYNQMMVKAGLNDDMERNLIQNAHAVERILL
AATDDKKTEFQKKKNARDVKEGKEEIDHNKTGGTFYKMVRDDKTIYFSPIRITFLKEEVKT
MYKTTMGSDGFSGLNHIMIGHSQMNDVCFQRSKALKRVGLDPSLISTFAGSTVPRRSGATGV
AIKGGGTLVAEAIRFIGRAMADRGLLRDIKAKTAYEKILLNLKNKCSAPQQKALVDQVIGSRN
PGIADIEDLTLLARSMVVVRPSVASKVVLPISIYAKIPQLGFNVEEYSMVGYEAMALYNMATP
VSILRMGDDAKDKSQLFFMSCFGAAYEDLRVLSALTGTEFKPRSALKCKGFHVPAKEQVEGMGA
ALMSIKLQFWAPMTRSGGNEVGGDGGSGQISCSPVFAVERPIALSKQAVRRMLSMNIEGRDADV
KGNLLKMMNDSMAKKTSGNAFIGKKMFQISDKNKTNPIEIPIKQTIPNFFFGRDTAEDYDDLDYLE.
Background
Influenza B virus, often overshadowed by its influenza A counterpart, remains a substantial contributor to seasonal influenza infections and poses a considerable public health challenge. In the quest for effective countermeasures, Influenza B Virus Nucleoprotein Recombinant has emerged as a focal point in the ongoing battle against this resilient virus. This research endeavors to unveil the intricacies of the Nucleoprotein Recombinant, delving into its structural nuances, immunogenic capabilities, and applications in vaccine development and antiviral therapies. By dissecting the properties of the Nucleoprotein Recombinant, scientists aspire to fortify our defenses against Influenza B, potentially reshaping strategies for broader influenza immunity.
Structural Insights into Nucleoprotein Recombinant:
Engineered to replicate key viral components, the Influenza B Virus Nucleoprotein Recombinant serves as a molecular mirror, allowing a comprehensive study of the virus's genetic material. Understanding its three-dimensional structure and conformational intricacies is crucial, not only for decoding the virus's replication mechanisms but also for tailoring interventions like vaccines and antiviral drugs to specific vulnerabilities.
Immunogenic Potential and Vaccine Development:
The challenge of Influenza B's seasonal variability necessitates innovative approaches to vaccine development. Nucleoprotein Recombinant, designed to induce potent immune responses, emerges as a promising candidate. By presenting conserved viral elements to the immune system, the recombinant protein seeks to instigate robust and durable immunity, countering the virus's propensity for antigenic drift and promoting broader protection.
Application in Antiviral Therapies:
In addition to its role in vaccination, the Influenza B Virus Nucleoprotein Recombinant holds potential in antiviral therapies. The recombinant protein's ability to provoke immune responses can be harnessed for the development of immunotherapies. Monoclonal antibodies derived from the Nucleoprotein Recombinant may offer targeted treatments, providing a dynamic approach to mitigating the impact of Influenza B infections.
Challenges and Future Directions:
Despite the promises held by the Nucleoprotein Recombinant, challenges persist. The virus's ability to undergo genetic reassortment and antigenic drift requires ongoing vigilance and adaptability in recombinant strategies. Considerations of vaccine safety, efficacy, and public acceptance demand continual exploration to optimize the translational success of Nucleoprotein Recombinant-based interventions.
Influenza B Virus Nucleoprotein Recombinant stands as a beacon in the scientific quest against influenza, offering a pathway to a more comprehensive and resilient immunity. Its structural insights, immunogenic potential, and applications in vaccine development and antiviral therapies position it as a central player. As researchers delve deeper into the molecular intricacies of Nucleoprotein Recombinant, they not only fortify our defenses against Influenza B but potentially pave the way for a paradigm shift in our approach to influenza prevention and control, influencing the landscape of global health preparedness.

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:

AITRL Human Recombinant, T7 Tag

Osteostat, TNFSF18, Activation-induced TNFR member Ligand, GITRL,TL6, AITRL, Glucocorticoid-induced TNF-related ligand, hGITRL, Tumor necrosis factor ligand superfamily member 18, MGC138237.

Product # :

CYT-807

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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description
source
formulation
purity
More Info

Description

AITRL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 134 amino acids (81-199 a.a) and having a molecular mass of 15kDa.AITRL is fused to a 15 amino acid T7-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Osteostat is the cytokine that binds to TNFRSF18/AITR/GITR and is important for interactions between activated T-lymphocytes and endothelial cells and may modulate T-lymphocyte survival in peripheral tissues. Osteostat is expressed at high levels in the small intestine, ovary, testis, kidney and endothelial cells after stimulation by lipopolysaccharides.
Osteostat protein is detectable in human microvascular EC and is highly up-regulated by IFN-alpha and IFN-beta. Osteostat inhibit differentiation of osteoclasts from monocytic precursor cells. Osteostat suppresses the early stage of osteoclastogenesis via inhibition of macrophage colony-stimulating factorinduced receptor activator of NF-kappaB (RANK) expression in the osteoclast precursor cells. Osteostat does not inhibit lipopolysaccharide-induced RANK expression in monocytes and dendritic cells, or activation-induced RANK expression in T cells. Osteostat is a novel regulator of osteoclast generation and substantiate the major role played by the endothelium in bone physiology.
Synonyms
Osteostat, TNFSF18, Activation-induced TNFR member Ligand, GITRL,TL6, AITRL, Glucocorticoid-induced TNF-related ligand, hGITRL, Tumor necrosis factor ligand superfamily member 18, MGC138237.
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
MASMTGGQQM GRGSHMAKFG PLPSKWQMAS SEPPCVNKVS DWKLEILQNG LYLIYGQVAP NANYNDVAPF EVRLYKNKDM IQTLTNKSKI QNVGGTYELH VGDTIDLIFN SEHQVLKNNT YWGIILLANP QFIS.
Background
What is the molecular weight/Mw of AITRL Protein?
AITRL Protein has a total Mw of 15kDa.

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

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

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

What is the amino acid sequence of AITRL Protein?
MASMTGGQQM GRGSHMAKFG PLPSKWQMAS SEPPCVNKVS DWKLEILQNG LYLIYGQVAP NANYNDVAPF EVRLYKNKDM IQTLTNKSKI QNVGGTYELH VGDTIDLIFN SEHQVLKNNT YWGIILLANP QFIS.

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

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

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